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1.
Curr Treat Options Cardiovasc Med ; 22(2): 5, 2020 Feb 03.
Article in English | MEDLINE | ID: mdl-32016641

ABSTRACT

PURPOSE OF THE REVIEW: This review will explore frequently encountered diagnostic challenges and summarize the role cardiac imaging plays in defining the boundaries of what constitutes the athlete's heart syndrome versus pathology. RECENT FINDINGS: Investigations have predominantly focused on differentiating the athlete's heart from potentially lethal pathological conditions that may produce a similar cardiac morphology. Guidelines have identified criteria for identifying definitive pathology, but difficulty arises when individuals fall in the gray zone of expected athletic remodeling and pathology. Transthoracic echo has traditionally been the imaging modality of choice utilizing parameters such as wall thickness, wall:volume ratio, and certain diastolic parameters. Newer echocardiogram techniques such as strain imaging and speckle tracking have potential additive utility but still need further investigation. Cardiac magnetic resonance (CMR) imaging has emerged as an additive technique to help differentiate the phenotypic overlap between these groups. Utilizing gadolinium enhancement and T1 mapping along with its excellent spatial resolution can help distinguish pathology from physiology. Both established and novel cardiac imaging modalities have been used for uncovering the at risk athletes with cardiomyopathies. The issue is of practical importance because athletes are frequently referred to the cardiologist with symptoms of fatigue, palpitations, presyncope, and/or syncope concerned about the safety of their future participation. Imaging is a key component of risk stratification and identifying normal findings of the developed athlete and those "at-risk" athletes.

2.
Small ; 12(2): 169-73, 2016 Jan 13.
Article in English | MEDLINE | ID: mdl-26573881

ABSTRACT

Rectangular DNA origami functionalized with thiols in each of the four corners immobilizes by self-assembly between lithographically patterned gold nanodots on a silicon oxide surface.


Subject(s)
DNA/chemistry , Gold/chemistry , Metal Nanoparticles/chemistry , Nucleic Acid Conformation , DNA/ultrastructure , Metal Nanoparticles/ultrastructure , Microscopy, Atomic Force
3.
Nanoscale ; 7(37): 15495-506, 2015 Oct 07.
Article in English | MEDLINE | ID: mdl-26274368

ABSTRACT

A helical hexapeptide was designed to link in a rigid parallel orientation to a gold surface. The peptide sequence of the newly synthesized compound is characterized by the presence of two 4-amino-1,2-dithiolane-4-carboxylic acid (Adt) residues (positions 1 and 4) to promote a bidentate interaction with the gold surface, two L-Ala residues (positions 2 and 5) and two-aminoisobutyric acid (Aib) residues (positions 3 and 6) to favor a high population of the 310-helix conformation. Furthermore, a ferrocenoyl (Fc) probe was inserted at the N-terminus to investigate the electronic conduction properties of the peptide. X-Ray photoelectron spectroscopy and scanning tunneling microscopy techniques were used to characterize the binding of the peptide to the gold surface and the morphology of the peptide layer, respectively. Several electrochemical (cyclic voltammetry, chronoamperometry, square wave voltammetry) techniques were applied to analyze the electrochemical activity of the Fc probe, along with the influence of the peptide 3D-structure and the peptide layer morphology on electron transfer processes.


Subject(s)
Gold/chemistry , Molecular Probes/chemistry , Peptides/chemistry , Amino Acids/chemistry , Surface Properties , Thiophenes/chemistry , X-Ray Diffraction
4.
Arch Phys Med Rehabil ; 96(3 Suppl): S46-53, 2015 Mar.
Article in English | MEDLINE | ID: mdl-25721547

ABSTRACT

OBJECTIVE: To evaluate the feasibility and usability of an assistive technology (AT) prototype designed to be operated with conventional/alternative input channels and a P300-based brain-computer interface (BCI) in order to provide users who have different degrees of muscular impairment resulting from amyotrophic lateral sclerosis (ALS) with communication and environmental control applications. DESIGN: Proof-of-principle study with a convenience sample. SETTING: An apartment-like space designed to be fully accessible by people with motor disabilities for occupational therapy, placed in a neurologic rehabilitation hospital. PARTICIPANTS: End-users with ALS (N=8; 5 men, 3 women; mean age ± SD, 60 ± 12 y) recruited by a clinical team from an ALS center. INTERVENTIONS: Three experimental conditions based on (1) a widely validated P300-based BCI alone; (2) the AT prototype operated by a conventional/alternative input device tailored to the specific end-user's residual motor abilities; and (3) the AT prototype accessed by a P300-based BCI. These 3 conditions were presented to all participants in 3 different sessions. MAIN OUTCOME MEASURES: System usability was evaluated in terms of effectiveness (accuracy), efficiency (written symbol rate, time for correct selection, workload), and end-user satisfaction (overall satisfaction) domains. A comparison of the data collected in the 3 conditions was performed. RESULTS: Effectiveness and end-user satisfaction did not significantly differ among the 3 experimental conditions. Condition III was less efficient than condition II as expressed by the longer time for correct selection. CONCLUSIONS: A BCI can be used as an input channel to access an AT by persons with ALS, with no significant reduction of usability.


Subject(s)
Amyotrophic Lateral Sclerosis/rehabilitation , Brain-Computer Interfaces , Disabled Persons/rehabilitation , Self-Help Devices , Aged , Communication Aids for Disabled , Electroencephalography , Environment , Female , Humans , Male , Middle Aged , Rehabilitation Centers , User-Computer Interface
5.
J Phys Chem A ; 118(33): 6674-84, 2014 Aug 21.
Article in English | MEDLINE | ID: mdl-24901672

ABSTRACT

Photoinduced electron transfer (PET) experiments have been carried out on peptide self-assembled monolayers (SAM) chemisorbed on a gold substrate. The oligopeptide building block was exclusively formed by C(α)-tetrasubstituted α-aminoisobutyric residues to attain a helical conformation despite the shortness of the peptide chain. Furthermore, it was functionalized at the C-terminus by a pyrene choromophore to enhance the UV photon capture cross-section of the compound and by a lipoic group at the N-terminus for linking to gold substrates. Electron transfer across the peptide SAM has been studied by photocurrent generation experiments in an electrochemical cell employing a gold substrate modified by chemisorption of a peptide SAM as a working electrode and by steady-state and time-resolved fluorescence experiments in solution and on a gold-coated glass. The results show that the electronic flow through the peptide bridge is strongly asymmetric; i.e., PET from the C-terminus to gold is highly favored with respect to PET in the opposite direction. This effect arises from the polarity of the Au-S linkage (Au(δ+)-S(δ-), junction effect) and from the electrostatic field generated by the peptide helix.


Subject(s)
Electrons , Gold/chemistry , Peptides/chemistry , Electrochemical Techniques , Electrodes , Electron Transport , Molecular Conformation , Photochemical Processes , Spectrometry, Fluorescence
6.
J Pept Sci ; 20(7): 494-507, 2014 Jul.
Article in English | MEDLINE | ID: mdl-24845474

ABSTRACT

Interactions between peptides are relevant from a biomedical point of view, in particular for the role played by their aggregates in different important pathologies, and also because peptide aggregates represent promising scaffolds for innovative materials. In the present article, the aggregation properties of the homo-peptides formed by α-aminoisobutyric acid (U) residues are discussed. The peptides investigated have chain lengths between six and 15 residues and comprise benzyl and naphthyl groups at the N- and C-termini, respectively. Spectroscopic experiments and molecular dynamics simulations show that the shortest homo-peptide, constituted by six U, does not exhibit any tendency to aggregate under the conditions examined. On the other hand, the homologous peptide with 15 U forms very stable and compact aggregates in 70/30(v/v) methanol/water solution. Atomic force microscopy images indicate that these aggregates promote formation of long fibrils once they are deposited on a mica surface. The aggregation phenomenon is mainly due to hydrophobic interactions occurring between very stable helical structures, and the aromatic groups in the peptides seem to play a minor role.


Subject(s)
Aminoisobutyric Acids/chemistry , Molecular Dynamics Simulation , Oligopeptides/chemistry , Microscopy, Atomic Force , Protein Aggregates , Protein Interaction Domains and Motifs , Protein Structure, Quaternary , Protein Structure, Secondary
7.
Soft Matter ; 10(15): 2508-19, 2014 Apr 21.
Article in English | MEDLINE | ID: mdl-24647758

ABSTRACT

The aggregation properties of two Ala-based pentapeptides were investigated by spectroscopic techniques and molecular dynamics (MD) simulations. The two peptides, both functionalized at the N-terminus with a pyrenyl group, differ in the insertion of an α-aminoisobutyric acid residue at position 4. We showed that this single modification of the homo-peptide sequence inhibits the aggregation of the pentapeptide in aqueous solutions. Atomic force microscopy imaging revealed that the two peptides form mesoscopic aggregates of very different morphologies when deposited on mica. MD experiments showed that the two peptides have a very different propensity to form ß-pleated sheet structures, as confirmed by our spectroscopic measurements. The implications of these findings for our understanding of the mechanism leading to the formation of amyloid structures, primary responsible for numerous neurodegenerative diseases, are also discussed.


Subject(s)
Alanine/chemistry , Molecular Dynamics Simulation , Peptides/chemistry , Hydrogen Bonding , Methanol/chemistry , Microscopy, Atomic Force , Peptides/metabolism , Protein Structure, Secondary , Water/chemistry
8.
Chemphyschem ; 15(1): 64-8, 2014 Jan 13.
Article in English | MEDLINE | ID: mdl-24273084

ABSTRACT

A bioinspired approach is applied to photoelectric conversion devices. A 3(10)-helical hexapeptide bearing a pyrene unit is immobilized on a gold-covered TiO2 surface. The device is integrated for the first time in a dye-sensitized solar cell, exhibiting stability after several measurements. The approach could have promising applications in the field of optoelectronics.


Subject(s)
Biomimetic Materials/chemistry , Gold/chemistry , Peptides/chemistry , Solar Energy , Titanium/chemistry , Biomimetics/methods , Coloring Agents/chemistry , Protein Conformation
9.
Nanotechnology ; 23(25): 255304, 2012 Jun 29.
Article in English | MEDLINE | ID: mdl-22652812

ABSTRACT

We report on the use of spider fibers as micro- and nanostencils for the fabrication of nanogaps between ultrathin conductive electrodes, and as molds for fabrication of micro- and nanowires by deposition of evaporated gold. Atomic force microscopy (AFM) morphological characterization of the nanogaps is described, together with the measurement of the electrical behavior of both nanogaps and nanowires. Gaps as narrow as 20 nm, comparable to e-beam-fabricated gaps, with electrical resistance higher than 10(13) Ω have been obtained; while conductive fibers ranging from 350 nm to 1.5 µm in diameter and resistances ranging from 50 MΩ to 100 Ω have been obtained and characterized.


Subject(s)
Nanotechnology/instrumentation , Nanotechnology/methods , Nanowires/chemistry , Silk/chemistry , Spiders , Animals , Electric Conductivity , Gold/chemistry , Microscopy, Atomic Force , Microscopy, Electron, Scanning , Nanowires/ultrastructure
10.
J Pept Sci ; 17(2): 124-31, 2011 Feb.
Article in English | MEDLINE | ID: mdl-21234984

ABSTRACT

The photocurrent generation properties of mono- and bi-component peptide-based self-assembled monolayers (SAMs) immobilized on a gold surface were studied by electrochemical and spectroscopic techniques. The peptides investigated comprised almost exclusively C-tetrasubstituted -amino acids. These non-coded residues, because of their unique conformational properties, forced the peptide backbone to attain a helical conformation, as confirmed by X-ray crystal structure and CD determinations in solution. The peptide helical structure promoted the formation of a stable SAM on the gold surface, characterized by an electric macrodipole directed from the C(δ−) to the N(δ+) terminus, that remarkably affected the electron transfer (ET) process through the peptide chain. The peptides investigated were derivatized with chromophores strongly absorbing in the UV region to enhance the efficiency of the photocurrent generation (antenna effect). The influence of the nature of the peptide­gold interface on the ET process (junction effect) was analyzed by comparing the photocurrent generation process in peptide SAMs immobilized on a gold surface through AuS linkages with that in a bi-component SAM embedding a photoactive peptide into the linked palisade formed by disulfide-functionalized peptides.


Subject(s)
Gold/chemistry , Peptides/chemistry , Photochemistry/methods
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