Creating stabilized peptide mimics of the collagen triple helix is challenging, especially for collagen heterotrimers. Interstrand sidechain crosslinking offers a useful approach, though this strategy can suffer from destabilizing structural perturbations, sequence limitations and synthetic complexity. Herein, we show that the geometry of hydrogen bonding in the collagen triple helix is compatible with installation of terminal β-turn-mimicking linkers at the N-terminal and C-terminal ends of the triple helix. These double-turn-containing collagen peptide mimics fold into highly stable, intramolecular triple helical structures, providing access to profoundly miniaturized triple helix mimics. Intramolecular triple helix formation exhibits significantly accelerated folding kinetics. Comprehensive kinetic analysis reveals that the rate-limiting step of folding is distinct at low and high temperatures, affording unique insight into the mechanism.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1002/cbic.202400834 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Solid-State NMR Spectroscopy Investigation of Structural Changes of Mechanically Strained Mouse Tail Tendons.
J Am Chem Soc
March 2025
Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, United Kingdom.
Structural tissues like tendon are subjected to repeated tensile strains and excessive strains cause irreversible changes to the tissue. Large strains affect the molecular structure and organization of the extracellular matrix, and these are the parameters that drive cell behavior, including tissue repair. Here we describe a method to perform solid-state NMR spectroscopy on strained tissue samples under magic-angle spinning to achieve high-resolution NMR spectra while maintaining the tissue's native hydration state.
View Article and Find Full Text PDFRational designation and characterization of a novel humanized collagen capable of self-assembling into triple helix and fibrils with D-period.
Protein Expr Purif
March 2025
State Key Laboratory of Biopharmaceutical Preparation and Delivery, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, PR China; University of Chinese Academy of Sciences, Beijing 100049, PR China. Electronic address:
The triple helix and D-period are distinctive features of native collagen, crucial for its physicochemical properties and bioactivities. However, developing recombinant humanized collagen with D-period features remains elusive. Here, we present a strategy for preparing a novel recombinant humanized collagen using a 'charged-hydrophobic-charged amino acid' sequence with the capacity of self-assembling.
View Article and Find Full Text PDFCOL1A1 and COL1A2 Gene Variants Causing Osteogenesis Imperfecta in a Major Referral Center of India.
Am J Med Genet A
March 2025
Department of Paediatric Orthopaedics, Christian Medical College, Vellore, Tamil Nadu, India.
Heterozygous COL1A1 and COL1A2 gene variants are known to cause osteogenesis imperfecta (OI) in 90% of the patients in the Western and Japanese populations. Two previous Indian reports, a total of 49 patients, showed their proportion in the Indian population to be 44% and 71%. We studied a population of 210 children with a clinical diagnosis of OI and focused on the cohort of children with (likely) pathogenic COL1A1/COL1A2 variants.
View Article and Find Full Text PDFA Collagen Triple Helix without the Superhelical Twist.
ACS Cent Sci
February 2025
Department of Chemistry, Rice University, 6100 Main Street, Houston, Texas 77005, United States.
Collagens are ubiquitous in biology: functioning as the backbone of the extracellular matrix, forming the primary structural components of key immune system complexes, and fulfilling numerous other structural roles in a variety of systems. Despite this, there is limited understanding of how triple helices, the basic collagen structural units, pack into collagenous assemblies. Here we use a peptide self-assembly system to design collagenous assemblies based on the C1q collagen-like region.
View Article and Find Full Text PDFβ-Turn Mimicking Crosslinking Provides Hyperstability and Fast Folding Kinetics for Short Collagen Triple Helices.
Chembiochem
February 2025
University of Pennsylvania, Chemistry, 231 South 34th Street, 19104-6323, Philadelphia, UNITED STATES OF AMERICA.
Creating stabilized peptide mimics of the collagen triple helix is challenging, especially for collagen heterotrimers. Interstrand sidechain crosslinking offers a useful approach, though this strategy can suffer from destabilizing structural perturbations, sequence limitations and synthetic complexity. Herein, we show that the geometry of hydrogen bonding in the collagen triple helix is compatible with installation of terminal β-turn-mimicking linkers at the N-terminal and C-terminal ends of the triple helix.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!