The design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II (PPII) helices, such as those found in collagen, remains relatively limited. In this study, we focused on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen SP-A as a model. By dissecting the sequence derived from SP-A and synthesizing short collagen-like peptides, we successfully constructed a discrete bundle of hollow triple helices. Mutation studies pinpointed amino acid sequences, including hydrophobic and charged residues that are critical for oligomer formation. These insights guided the design of collagen-like peptides, resulting in the formation of diverse quaternary structures, including discrete and heterogenous bundled oligomers, 2D nanosheets, and pH-responsive nanoribbons. Our study represents a significant advancement in the understanding and harnessing of collagen higher-order assemblies beyond the triple helix.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11118445 | PMC |
| http://dx.doi.org/10.1101/2024.05.14.594194 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Analysis of the Effect of Human Type I Collagen-Derived Peptide on Bone Regenerative Capacity and Comparison with Various Collagen Materials In Vivo.
Medicina (Kaunas)
January 2025
Department of Plastic and Reconstructive Surgery, Niigata University Graduate School of Medical and Dental Sciences, Niigata 951-8510, Japan.
: Autologous bone grafting is the first choice for reconstructive surgery in bone defects due to trauma or malignant tumors. However, there is an increasing demand for minimally invasive alternatives involving bone regeneration using artificial materials. Biomimetic materials that replicate the body's microscopic structure, such as Cellnest, are gaining attention.
View Article and Find Full Text PDFDextromethorphan inhibits collagen and collagen-like cargo secretion to ameliorate lung fibrosis.
Sci Transl Med
December 2024
Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, 69117 Heidelberg, Germany.
Excessive deposition of fibrillar collagen in the interstitial extracellular matrix (ECM) of human lung tissue causes fibrosis, which can ultimately lead to organ failure. Despite our understanding of the molecular mechanisms underlying the disease, no cure for pulmonary fibrosis has yet been found. We screened a drug library and found that dextromethorphan (DXM), a cough expectorant, reduced the amount of excess fibrillar collagen deposited in the ECM in cultured primary human lung fibroblasts, a bleomycin mouse model, and a cultured human precision-cut lung slice model of lung fibrosis.
View Article and Find Full Text PDFAssembly of Recombinant Proteins into β-Sheet Fibrillating Peptide-Driven Supramolecular Hydrogels for Enhanced Diabetic Wound Healing.
ACS Biomater Sci Eng
January 2025
Inner Mongolia Key Laboratory for Molecular Regulation of the Cell, School of Life Sciences, Inner Mongolia University, Hohhot 010020, PR China.
Supramolecular hydrogels offer a noncovalent binding platform that preserves the bioactivity of structural molecules while enhancing their stability, particularly in the context of diabetic wound repair. In this study, we developed protein-peptide-based supramolecular hydrogels by assembling β-sheet fibrillizing peptides (designated Q11) with β-tail fused recombinant proteins. The Q11 peptides have the ability to drive the gradated assembly of N- or C-terminal β-sheet structure (β-tail) fused recombinant proteins.
View Article and Find Full Text PDFExploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix.
Nat Commun
November 2024
Department of Chemistry, Rice University, Houston, TX, USA.
The de novo design of self-assembling peptides has garnered significant attention in scientific research. While alpha-helical assemblies have been extensively studied, exploration of polyproline type II helices, such as those found in collagen, remains relatively limited. In this study, we focus on understanding the sequence-structure relationship in hierarchical assemblies of collagen-like peptides, using defense collagen Surfactant Protein A as a model.
View Article and Find Full Text PDFNoveland rapid self-gelation recombinant collagen-like protein hydrogel for wound regeneration: mediated by metal coordination crosslinking and reinforced by electro-oxidized tea polyphenols.
Biofabrication
November 2024
CAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, No. 189, Songling Road, Qingdao 266101, People's Republic of China.
Recombinant collagen holds immense potential in the development of medical functional materials, yet its widespread application remains hindered by the absence of a suitable self-assembly strategy. In this article, we report the discovery that the bacterial-derived collagen-like (CL) protein Scl2 can rapidly self-gelation (∼1 min at pH ∼7) due to properties enabled by metal coordination crosslinking. This was achieved by fusing metal ion chelating peptides to both termini of the protein.
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!