RESUMO
Nature uses elaborate methods to control protein assembly, including that of heterotrimeric collagen. Here, we established design principles for the composition and register-selective assembly of synthetic collagen heterotrimers. The assembly code enabled the self-sorting of eight different strands into threeâout of 512 possibleâtriple helices via complementary (4S)-aminoproline and aspartate residues. Native ESI-MS corroborated the specific assembly into coexisting heterotrimers.
Assuntos
Ácido Aspártico , Colágeno , Multimerização Proteica , Colágeno/química , Movimento CelularRESUMO
Nature uses salt bridges to control the folding and stability of many proteins, including collagen, the key structural protein in mammals. Here, we present an interstrand salt bridge between (4S)-aminoproline (Amp) and aspartic acid (Asp) that directs the composition and register-specific assembly of synthetic collagen heterotrimers. This Amp-Asp salt bridge allowed for the rational design of strands that fold into A2B and ABC-type heterotrimers with only three salt bridges per triple helix. Native ESI-MS and NMR spectroscopic analyses corroborated the specific assembly of the ABC heterotrimer.