A Lateral Salt Bridge for the Specific Assembly of an ABC-Type Collagen Heterotrimer
Nina B. Hentzen, Valdrin Islami, Martin Köhler, Renato Zenobi, Helma Wennemers
Abstract
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.
Topics & Concepts
ChemistrySalt bridgeSalt (chemistry)Aspartic acidFolding (DSP implementation)Bridge (graph theory)Helix (gastropod)StereochemistryBiophysicsBiochemistryCombinatorial chemistryAmino acidMutantOrganic chemistryAnatomyEcologyMedicineElectrical engineeringSnailBiologyEngineeringGeneCollagen: Extraction and CharacterizationChemical Synthesis and AnalysisMarine Biology and Environmental Chemistry