Designing Pathway-Controlled Multicomponent Ultrashort Peptide Hydrogels with Diverse Functionalities at the Nanoscale for Directing Cellular Behavior.

Tuning self-assembling pathways by implementing different external stimuli has been extensively studied, owing to their effective control over structural and mechanical properties. Consequently, multicomponent peptide hydrogels with high structural tunability and stimuli responsiveness are crucial in dictating cellular behavior. Herein, we have implemented both coassembly approach and pathway-dependent self-assembly to design nonequilibrium nanostructures to understand the thermodynamic and kinetic aspects of peptide self-assembly toward controlling cellular response. Our system involved an ultrashort peptide gelator and a hydrophilic surfactant which coassembled through different pathways, i.e., heat-cool and sonication methods with variable energy input. Interestingly, it was possible to access diverse structural and mechanical properties at the nanoscale in a single coassembled system. Further, the hydrophilic surfactant provided additional surface functionalities, thus creating an efficient hydrophilic matrix for cellular interaction. Such diverse functionalities in a single coassembled system could lead to the development of advanced scaffolds, with applications in various biomedical fields.

Conformation Controlled Hydrogelation of Minimalistic α, γ Hybrid Peptide.

A majority of short peptide (≤7 amino acids) hydrogels are primarily assembled via cross ß-structure formation. In contrast to the natural trend, herein, we report the formation of supramolecular hydrogel from the ultrashort hybrid folded peptide composed of canonical α-amino acid and noncanonical γ-amino acid, Fmoc-γPhe-Phe-OH. The designed hybrid peptide hydrogel is composed of entangled fibers, has viscoelastic properties, exhibits proteolytic stability, and exhibits cytocompatibility with L929 fibroblast cells. Mutating the peptide sequence by altering the position of γPhe from the N-termini to C-termini transforms the self-assembly into crystalline aggregates. Combining FTIR, 2D NMR, and DFT calculations revealed that the hydrogel-forming peptide adopts a C9 H-bonded conformation, resembling the well-known γ-turn. However, the isomeric hybrid peptide adopts an extended structure. The present study highlights the importance of secondary structure in the higher order assembly of minimalist hybrid peptides and broadens the range of secondary structures to design short peptide-based hydrogels.

Exploring a Solvent Dependent Strategy to Control Self-Assembling Behavior and Cellular Interaction in Laminin-Mimetic Short Peptide based Supramolecular Hydrogels.

Self-assembled hydrogels, fabricated through diverse non-covalent interactions, have been extensively studied in regenerative medicines. Inspired from bioactive functional motifs of ECM protein, short peptide sequences have shown remarkable abilities to replicate the intrinsic features of the natural extracellular milieu. In this direction, we have fabricated two short hydrophobic bioactive sequences derived from the laminin protein i. e., IKVAV and YIGSR. Based on the substantial hydrophobicity of these peptides, we selected a co-solvent approach as a suitable gelation technique that included different concentrations of DMSO as an organic phase along with an aqueous solution containing 0.1 % TFA. These hydrophobic laminin-based bioactive peptides with limited solubility in aqueous physiological environment showed significantly enhanced solubility with higher DMSO content in water. The enhanced solubility resulted in extensive intermolecular interactions that led to the formation of hydrogels with a higher-order entangled network along with improved mechanical properties. Interestingly, by simply modulating DMSO content, highly tunable gels were accessed in the same gelator domain that displayed differential physicochemical properties. Further, the cellular studies substantiated the potential of these laminin-derived hydrogels in enhancing cell-matrix interactions, thereby reinforcing their applications in tissue engineering.

Designing Cardin-Motif Peptide and Heparin-Based Multicomponent Advanced Bioactive Hydrogel Scaffolds to Control Cellular Behavior.

Recently, peptide and sugar-based multicomponent systems have gained much interest in attaining the sophisticated structure and biofunctional complexity of the extracellular matrix (ECM). To this direction, we have designed for the first time a biologically relevant minimalist Cardin-motif peptide capable of binding ECM-derived glycosaminoglycans. Herein, we explored Cardin-motif peptide and heparin-based biomolecular matrix by employing simple noncovalent interactions at the molecular level. Interestingly, this peptide was inadequate to induce hydrogelation at ambient pH due to the presence of basic amino acids. However, addition of heparin successfully triggered its gelation at physiological pH following favorable electrostatic interactions with heparin. Importantly, the newly developed scaffolds displayed tunable nanofibrous morphology and superior mechanical properties as controlled simply by the differential mixing ratio of both biomolecular entities. Additionally, these composite scaffolds could closely mimic the complexity of ECM as they demonstrated superior biocompatibility and enhanced growth and proliferation of neural cells as compared to the peptide scaffold.

Designing ECM-inspired supramolecular scaffolds by utilizing the interactions between a minimalistic neuroactive peptide and heparin.

Short bioactive peptide-based supramolecular hydrogels are emerging as interesting candidates for developing scaffolds for tissue engineering applications. However, proteins and peptides represent only a single class of molecules present in the native ECM, thus, recapitulating the complete ECM microenvironment via only peptide-based biomaterials is extremely challenging. In this direction, complex multicomponent-based biomaterials have started gaining importance for achieving the biofunctional complexity and structural hierarchy of the native ECM. Sugar-peptide complexes can be explored in this direction as they provide essential biological signaling required for cellular growth and survival in vivo. In this direction, we explored the fabrication of an advanced scaffold by employing heparin and short bioactive peptide interactions at the molecular level. Interestingly, the addition of heparin into the peptide has significantly modulated the supramolecular organization, nanofibrous morphology and the mechanical properties of the scaffold. Additionally, the combined hydrogels demonstrated superior biocompatibility as compared to the peptide counterpart at certain ratios. These newly developed scaffolds were also observed to be stable under 3-D cell culture conditions and supported cellular adhesion and proliferation. Most importantly, the inflammatory response was also minimized in the case of combined hydrogels as compared to heparin. We expect that this approach of using simple non-covalent interactions between the ECM-inspired small molecules to fabricate biomaterials with improved mechanical and biological properties could advance the current knowledge on designing ECM mimetic biomaterials. Such an attempt would create a novel, adaptable and simplistic bottom-up strategy for the invention of new and more complex biomaterials of ECM origin with advanced functions.

Exploring Supramolecular Interactions between the Extracellular-Matrix-Derived Minimalist Bioactive Peptide and Nanofibrillar Cellulose for the Development of an Advanced Biomolecular Scaffold.

It has been increasingly evident over the last few years that bioactive peptide hydrogels in conjugation with polymer hydrogels are emerging as a new class of supramolecular materials suitable for various biomedical applications owing to their specificity, tunability, and nontoxicity toward the biological system. Despite their unique biocompatible features, both polymer- and peptide-based scaffolds suffer from certain limitations, which restrict their use toward developing efficient matrices for controlling cellular behavior. The peptide hydrogels usually form soft matrices with low mechanical strength, whereas most of the polymer hydrogels lack biofunctionality. In this direction, combining polymers with peptides to develop a conjugate hydrogel can be explored as an emergent approach to overcome the limitations of the individual components. The polymer will provide high mechanical strength, whereas the biofunctionality of the material can be induced by the bioactive peptide sequence. In this study, we utilized TEMPO-oxidized nanofibrillar cellulose as the polymer counterpart, which was co-assembled with a short N-cadherin mimetic bioactive peptide sequence, Nap-HAVDI, to fabricate an NFC-peptide conjugate hydrogel. Interestingly, the mechanical strength of the peptide hydrogel was found to be significantly improved by combining the peptide with the NFC in the conjugate hydrogel. The addition of the peptide into the NFC also reduced the pore size within NFC matrices, which further helped in improving cellular adhesion, survival, and proliferation. Furthermore, the cells grown on the NFC and NFC-peptide hybrid hydrogel demonstrated normal expression of cytoskeleton proteins, i.e., ß-tubulin in C6 cells and actin in L929 cells, respectively. The selective response of neuronal cells toward the specific bioactive peptide was further observed through a protein expression study. Thus, our study demonstrated the collective role of the cellulose-peptide composite material that revealed superior physical properties and biological response of this composite scaffold, which may open up a new platform for biomedical applications.

Cooperative Calcium Phosphate Deposition on Collagen-Inspired Short Peptide Nanofibers for Application in Bone Tissue Engineering.

In recent years, immense attention has been devoted over the production of osteoinductive materials. To this direction, collagen has a dominant role in developing hard tissues and plays a crucial role in the biomineralization of these tissues. Here, we demonstrated for the first time the potential of the shortest molecular pentapeptide domain inspired from collagen toward mineralizing hydroxyapatite on peptide fibers to develop bone-filling material. Our simplistic approach adapted the easy and facile route of introducing the metal ions onto the peptide nanofibers, displaying adsorbed glutamate onto the surface. This negatively charged surface further induces the nucleation of the crystalline growth of hydroxyapatite. Interestingly, nucleation and growth of the hydroxyapatite crystals lead to the formation of a self-supporting hydrogel to construct a suitable interface for cellular interactions. Furthermore, microscopic and spectroscopic investigations revealed the crystalline growth of the hydroxyapatite onto peptide fibers. The physical properties were also influenced by this crystalline deposition, as evident from the hierarchical organization leading to hydrogels with enhanced mechanical stiffness and improved thermal stability of the scaffold. Furthermore, the mineralized peptide fibers were highly compatible with osteoblast cells and showed increased cellular biomarkers production, which further reinforced the potential application toward effectively fabricating the grafts for bone tissue engineering.

Design and analysis of DDoS mitigating network architecture.

Distributed Denial of Service (DDoS) attacks have emerged as the top security threat with the rise of e-commerce in recent years. Volumetric attacks are the most common DDoS attacks that aim to overwhelm the victim's bandwidth. The current mitigation methods use reactive filtering techniques that are not magical and straightforward solutions. In this paper, we propose a network architecture based on the capability to address the threat of DDoS attacks. Physically Unclonable Functions (PUFs) have emerged as a promising solution in security. Motivated by the capability approach, we put forward a network architecture where the routers use Transient Effect Ring Oscillator PUF to generate and verify capabilities. This novel hardware-based solution, to address the problem, has reduced the computational overhead of capability generation. Additionally, the destination has complete control over the incoming traffic in the proposed architecture, resulting in uninterrupted communication with the legitimate clients regardless of the attacker traffic. The large-scale simulation on an open-source Network Simulator (NS-3) has shown that the proposed architecture efficiently mitigates DDoS attacks to a large extend. With our proposed architecture, the throughput was hardly affected when attacker traffic was varied from 10 to 80%.

Biomass-derived cellulose nanofibers and iron oxide-based nanohybrids for thermal insulation application.

In recent years, due to high energy consumption in the building sector and subsequent environmental issues, environment-friendly and cost-effective thermally insulating materials are in high demand to improve the energy efficiency of buildings. Current commercially available thermal insulating materials (polystyrene) always pose a challenge due to their non-biodegradability and poor insulating performance. To this end, biomass-derived aerogels are attracting significant interest as renewable and sustainable insulating materials. In this work, we have developed a facile strategy for synthesizing cellulose nanofibers from biomass-derived wood pulp as a cost-effective starting material by TEMPO-oxidation, and further incorporating iron oxide nanoparticles to make a nanohybrid. Interestingly, in these nanohybrids, the functional attributes like mechanical strength and flammability were improved to a great extent and thus overcoming the limitations of the commercially available thermal insulating materials in terms of their stability and durability. Most importantly, these nanohybrids demonstrated very low thermal conductivity, as low as 0.024 W m-1 K-1, indicating the better insulating potential of these nanohybrids as compared to other conventional insulating materials.

Exploring the TEMPO-Oxidized Nanofibrillar Cellulose and Short Ionic-Complementary Peptide Composite Hydrogel as Biofunctional Cellular Scaffolds.

Multicomponent self-assembly is an emerging approach in peptide nanotechnology to develop nanomaterials with superior physical and biological properties. Inspired by the multicomponent nature of the native extracellular matrix (ECM) and the well-established advantages of co-assembly in the field of nanotechnology, we have attempted to explore the noncovalent interactions among the sugar and peptide-based biomolecular building blocks as an approach to design and develop advanced tissue scaffolds. We utilized TEMPO-oxidized nanofibrillar cellulose (TO-NFC) and a short ionic complementary peptide, Nap-FEFK, to fabricate highly tunable supramolecular hydrogels. The differential doping of the peptide into the TO-NFC hydrogel was observed to tune the surface hydrophobicity, microporosity, and mechanical stiffness of the scaffold. Interestingly, a differential cellular response was observed toward composite scaffolds with a variable ratio of TO-NFC versus Nap-FEFK. Composite scaffolds having a 10:1 (w/w) ratio of TO-NFC and the Nap-FEFK peptide showed enhanced cellular survival and proliferation under two-dimensional cell culture conditions. More interestingly, the cellular proliferation on the 10:1 matrix was found to be similar to that of Matrigel in three-dimensional culture conditions, which clearly indicated the potential of these hydrogels in advanced tissue engineering applications. Additionally, these composite hydrogels did not elicit any significant inflammatory response in Raw cells and supported their survival and proliferation, which further emphasized their ability to form versatile scaffolds for tissue regeneration. This multicomponent assembly approach to construct biomolecular composite hydrogels to access superior physical and biological properties within the scaffold is expected to improve the scope for designing novel ECM-mimicking biomaterials for regenerative medicine.

Cooperative Metal Ion Coordination to the Short Self-Assembling Peptide Promotes Hydrogelation and Cellular Proliferation.

Noncovalent interactions among short peptides and proteins lead to their molecular self-assembly into supramolecular packaging, which provides the fundamental basis of life. These biomolecular assemblies are highly susceptible to the environmental conditions, including temperature, light, pH, and ionic concentration, and thus inspiring the fabrication of a new class of stimuli-responsive biomaterials. Here, for the first time the cooperative effect of the divalent metal ions to promote hydrogelation in the short collagen inspired self-assembling peptide for developing advanced biomaterials is reported. Introduction of the biologically relevant metal ions (Ca2+ /Mg2+ ) to the peptide surpasses its limitation to self-assemble into a multiscale structure at physiological pH. In particular, in presence of metal ions, the negatively charged peptide shows a distinct shift in its equilibrium point of gelation and demonstrates conversion from sol to gel and thus enabling the scope of fabricating an advanced biomaterial for controlling cellular behavior. Interestingly, tunable mechanical strength and improved cellular response are observed within ion-coordinated peptide hydrogels compared to the peptide gelator. Microscopic analyses, rheological assessment, and biological studies establish the importance of utilizing a novel strategy by simply using metal ions to modulate the physical and biological attributes of collagen inspired peptide (CIPs) to construct next-generation biomaterials.

Designing aromatic N-cadherin mimetic short-peptide-based bioactive scaffolds for controlling cellular behaviour.

The development of suitable biomaterials is one of the key factors responsible for the success of the tissue-engineering field. Recently, significant effort has been devoted to the design of biomimetic materials that can elicit specific cellular responses and direct new tissue formation mediated by bioactive peptides. The success of the design principle of such biomimetic scaffolds is mainly related to the cell-extracellular matrix (ECM) interactions, whereas cell-cell interactions also play a vital role in cell survival, neurite outgrowth, attachment, migration, differentiation, and proliferation. Hence, an ideal strategy to improve cell-cell interactions would rely on the judicious incorporation of a bioactive motif in the designer scaffold. In this way, we explored for the first time the primary functional pentapeptide sequence of the N-cadherin protein, HAVDI, which is known to be involved in cell-cell interactions. We have formulated the shortest N-cadherin mimetic peptide sequence utilizing a minimalistic approach. Furthermore, we employed a classical molecular self-assembly strategy through rational modification of the basic pentapeptide motif of N-cadherin, i.e. HAVDI, using Fmoc and Nap aromatic moieties to modify the N-terminal end. The designed N-cadherin mimetic peptides, Fmoc-HAVDI and Nap-HAVDI, self-assembled to form a nanofibrous network resulting in a bioactive peptide hydrogel at physiological pH. The nanofibrous network of the pentapeptide hydrogels resembles the topology of the natural ECM. Furthermore, the mechanical strength of the gels also matches that of the native ECM of neural cells. Interestingly, both the N-cadherin mimetic peptide hydrogels supported cell adhesion and proliferation of the neural and non-neural cell lines, highlighting the diversity of these peptidic scaffolds. Further, the cultured neural and non-neural cells on the bioactive scaffolds showed normal expression of ß-III tubulin and actin, respectively. The cellular response was compromised in control peptides, which further establishes the significance of the bioactive motifs towards controlling the cellular behaviour. Our study indicated that our designer N-cadherin-based peptidic hydrogels mimic the structural as well as the physical properties of the native ECM, which has been further reflected in the functional attributes offered by these scaffolds, and thus offer a suitable bioactive domain for further use as a next-generation material in tissue-engineering applications.

An overview of latest advances in exploring bioactive peptide hydrogels for neural tissue engineering.

Neural tissue engineering holds great potential in addressing current challenges faced by medical therapies employed for the functional recovery of the brain. In this context, self-assembling peptides have gained considerable interest owing to their diverse physicochemical properties, which enable them to closely mimic the biophysical characteristics of the native ECM. Additionally, in contrast to synthetic polymers, which lack inherent biological signaling, peptide-based nanomaterials could be easily designed to present essential biological cues to the cells to promote cellular adhesion. Moreover, injectability of these biomaterials further widens their scope in biomedicine. In this context, hydrogels obtained from short bioactive peptide sequences are of particular interest owing to their facile synthesis and highly tunable properties. In spite of their well-known advantages, the exploration of short peptides for neural tissue engineering is still in its infancy and thus detailed discussion is required to evoke interest in this direction. This review provides a general overview of various bioactive hydrogels derived from short peptide sequences explored for neural tissue engineering. The review also discusses the current challenges in translating the benefits of these hydrogels to clinical practices and presents future perspectives regarding the utilization of these hydrogels for advanced biomedical applications.

Enzyme-Induced Supramolecular Order in Pyrene Dipeptide Hydrogels for the Development of an Efficient Energy-Transfer Template.

Peptide self-assembly is gathering much attention due to the precise control it provides for the arrangement of functional moieties for the fabrication of advanced functional materials. It is desirable to use a physical, chemical, or biological trigger that can control the self-assembly process. In the current article, we have applied an enzyme to induce the peptide self-assembly of an aromatic peptide amphiphile, which modulates the supramolecular order in the final gel phase material. We accessed diverse peptide hydrogels from identical gelator concentrations by simply changing the enzyme concentration, which controlled the reaction kinetics and influenced the dynamics of self-assembly. Depending upon the concentration of the enzyme, a bell-shaped relationship was observed in terms of intermolecular interactions, morphology, and properties of the final gel phase material. The access of non-equilibrium structures was further demonstrated by fluorescence emission spectroscopy, circular dichroism spectroscopy, atomic force microscopy, transmission electron microscopy, and rheology. This strategy is applied to construct a charge-transfer hydrogel by doping the donor hydrogel with an acceptor moiety, which exhibits efficient energy transfer. Interestingly, such structural control at the nanoscopic level can further tune the energy-transfer efficiency by simply modulating the enzyme concentration.

Elastin-inspired supramolecular hydrogels: a multifaceted extracellular matrix protein in biomedical engineering.

The phenomenal advancement in regenerative medicines has led to the development of bioinspired materials to fabricate a biomimetic artificial extracellular matrix (ECM) to support cellular survival, proliferation, and differentiation. Researchers have diligently developed protein polymers consisting of functional sequences of amino acids evolved in nature. Nowadays, certain repetitive bioinspired polymers are treated as an alternative to synthetic polymers due to their unique properties like biodegradability, easy scale-up, biocompatibility, and non-covalent molecular associations which imparts tunable supramolecular architecture to these materials. In this direction, elastin has been identified as a potential scaffold that renders extensibility and elasticity to the tissues. Elastin-like polypeptides (ELPs) are artificial repetitive polymers that exhibit lower critical solution temperature (LCST) behavior in a particular environment than synthetic polymers and hence have gained extensive interest in the fabrication of stimuli-responsive biomaterials. This review discusses in detail the unique structural aspects of the elastin and its soluble precursor, tropoelastin. Furthermore, the versatility of elastin-like peptides is discussed through numerous examples that bolster the significance of elastin in the field of regenerative medicines such as wound care, cardiac tissue engineering, ocular disorders, bone tissue regeneration, etc. Finally, the review highlights the importance of exploring short elastin-mimetic peptides to recapitulate the structural and functional aspects of elastin for advanced healthcare applications.

Pathway-Dependent Preferential Selection and Amplification of Variable Self-Assembled Peptide Nanostructures and Their Biological Activities.

We demonstrate the formation of diverse peptide nanostructures, which are "out of equilibrium" based on a single dipeptide gelator. These structures represent the differential energy states of the free energy landscape, which are accessed by differential energy inputs provided by variable self-assembly pathways, that is, heat-cool method or ultrasonication. A higher energy input by the heat-cool method created a thermodynamically favored long entangled nanofibrillar network, while twisted ribbonlike structures were prevalent by ultrasonication. Interestingly, the nanofibrillar network representing the global thermodynamic minima could be accessed by simply melting the kinetically trapped structures as indicated by the thermoreversibility studies. The impact on the material strength was remarkable; gels with an order of magnitude difference in mechanical properties could be fabricated by simply modulating the self-assembly pathways. Interestingly, the thermodynamically favored nanofibrous network promoted cellular adhesion and survival, while a significant number of cells fail to adhere on the kinetically trapped twisted ribbons. Thus, nonequilibrium nanostructures open up new directions to develop advanced functional materials with diverse functions.

Accessing Highly Tunable Nanostructured Hydrogels in a Short Ionic Complementary Peptide Sequence via pH Trigger.

Creating diverse nanostructures from a single gelator through modulating the self-assembly pathway has been gaining much attention in recent years. To this direction, we are exploring the effect of modulation of pH as a potential self-assembly pathway in governing the physicochemical properties of the final gel phase material. In this context, we used a classical nongelator with the ionic complementary sequence FEFK, which was rationally conjugated to an aromatic group naphthoxyacetic acid (Nap) at the N-terminal end to tune its gelation behavior. Interestingly, the presence of oppositely charged amino acids in the peptide amphiphile resulted in pH-responsive behavior, leading to the formation of hydrogels over a wide pH range (2.0-12.0); however, their structures differ significantly at the nanoscale. Thus, by simply manipulating the overall charge over the exposed surface of the peptide amphiphiles as a function of pH, we were able to access diverse self-assembled nanostructures within a single gelator domain. The charged state of the gelator at the extreme pH (2.0, 12.0) led to a thinner fiber formation, in contrast to the thicker fibers observed near the physiological pH owing to charge neutralization, thus promoting the lateral association. Such variation in molecular packing was found to be further reflected in the variable mechanical strengths of the peptide hydrogels obtained at different pH values. Moreover, the gelation of the peptide at physiological pH offers an additional advantage to explore this hydrogel as a cell culture scaffold. We anticipate that our study on controlling the self-assembly pathway of the ionic complementary peptide amphiphile can be an elegant approach to access diverse self-assembled materials, which can expand the zone of its applicability as a stimuli-responsive biomaterial.

Triggering Supramolecular Hydrogelation Using a Protein-Peptide Coassembly Approach.

In recent years, the molecular self-assembly approach has witnessed a sudden surge in coassembly strategy to achieve extensive control over accessing diverse nanostructures and functions. To this direction, peptide-peptide coassembly has been explored to some extent in the literature, but protein-peptide coassembly is still in its infancy for controlling the self-assembling properties. To the best of our knowledge, our study illustrated the merits of protein-peptide coassembly toward inducing gelation to a nongelator dipeptide sequence, for the first time. This simplistic approach could provide access to diverse mechanical and structural properties within a single gelator domain at identical concentrations with a simple variation in the protein concentrations. Interestingly, the protein-peptide interactions could transform aggregate-like structures into fibrillar nanostructures. The study attempts to provide the proof of concept for the nonspecific protein-peptide interactions purely based on simple noncovalent interactions. The range of dissociation constants and binding energies obtained from bioloyer interferometry and docking studies confirmed the involvement of noncovalent interactions in protein-peptide coassembly, which triggers gelation. Moreover, different binding affinities of a protein toward an individual peptide essentially demonstrated a route to achieve precise control over differential self-assembling properties. Another important aspect of this study was entrapment of an enzyme protein within the gel network during coassembly without inhibiting enzyme activity, which can serve as a scaffold for catalytic reactions. The present study highlights the nonconventional way of protein-peptide interactions in triggering self-assembly in a nonassembling precursor. We anticipate that fundamental insights into the intermolecular interactions would lead to novel binary supramolecular hydrogels that can be developed as a next generation biomaterial for various biomedical applications.

Considerations for the nano aperture ion source: Geometrical design and electrical control.

A new type of ion source is being developed for proton beam writing and other focused ion beam applications. The potential of this source as well as achieved performance of the nano aperture ion source will be evaluated. Based on the ideal source parameters, critical geometrical parameters constraining chromatic aberrations and a possible pathway to achieve this performance will be presented. Finally, an electronic control system to minimize chromatic and spherical aberrations to an acceptable level will be demonstrated.

Tuning the gelation behavior of short laminin derived peptides via solvent mediated self-assembly.

Controlling the self-assembly pathways through solvent mediated approach can be an effective means to create complex, multifunctional structures. However, predicting the effect of solvent environment on both solubility of the monomer and their self-assembling behaviour remains a challenge. Our work mainly aims to understand the role of solvents in driving the supramolecular self-assembly of structurally related bioinspired pentapeptides (IKVAV and YIGSR), derived from native laminin protein. The exploration of the short sequences from this useful functional protein is still in its infancy. An N-terminal hydrophobic modification of IKVAV and YIGSR has been used to illustrate the gelator-gelator and gelator-solvent intermolecular interactions. Microscopic investigation of hydrophobic derivatives showed the transformation of fibrous morphology to sheet like structures, on varying solvent polarity from aqueous-organic mixture to aqueous solvent. Interestingly, these gels possess mechano-responsive and thermo-reversible properties, which also showed the remarkable solvent susceptibility. Our study clearly indicates that judicious choice of solvents may help in designing new soft materials with controlled properties, lesser defects and higher reproducibility.