In this double-blind clinical study, we evaluated the effect of our newly developed synthetic collagen-like hexapeptide on wrinkles. Twenty healthy women volunteers, aged 40 to 62 years old, participated in the study Volunteers applied either a gel formula containing 3% of the collagen-like peptide and 1% of a booster molecule that stimulates general cell metabolism with no specific effect on wrinkles, or a placebo gel, on the eye zone area twice a day for 4 weeks. Control visits were performed at the beginning and the end of the study. Skin wrinkles were evaluated clinically and by silicon replica analysis followed by statistical treatment using the matched-pairs Student's t-test. The results showed that application of the collagen-like peptide on the skin significantly reduced the total surface of wrinkles and this effect was observed in 75% of the replicas. Similarly, the decrease in number and average depth of wrinkles was also significant and was observed in 65% and 75% of the replicas, respectively. The effect of the collagen-like peptide on reducing the total and average length of wrinkles was also remarkable. This effect was statistically highly significant (p < 0.003) and was observed in 75% to 80% of the replicas. Moreover these results were supported by volunteer questionnaires and clinical observation. The results demonstrate that the collagen-like peptide acts deeply and intensely on wrinkles; these properties are of great interest in the field of antiaging skin care research.
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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 PDFACS 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 PDFNat 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 PDFBiofabrication
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 PDFbioRxiv
September 2024
Department of Chemistry, Rice University, 6100 Main Street, Houston, TX, 77005, USA.
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.
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