Academic Journal

Discovering potential anti-skin-aging peptides in collagen: computer-assisted rapid screening and structure–activity relationships.

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Discovering potential anti-skin-aging peptides in collagen: computer-assisted rapid screening and structure–activity relationships.
Συγγραφείς: Zhang, Ruihao, Li, Yang, Li, Yonghui, Zhang, Hui
Πηγή: Collagen & Leather; 9/1/2025, Vol. 7 Issue 1, p1-20, 20p
Θεματικοί όροι: Skin aging, Peptides, Enzyme inhibitors, Structure-activity relationships, Collagen, Data analysis, Dietary bioactive peptides, Machine learning
Περίληψη: The application of peptides as inhibitors of skin aging is a promising area of research. Previous researches have predominantly focused on extracting anti-aging peptides from the collagen of specific animals, while large-scale rapid screening and analysis of the structure–activity relationships of these peptides have been scarcely reported. In the present investigation, we developed a machine learning model for screening potential anti-skin-aging peptides (PASAPs), achieving a Matthews correlation coefficient (MCC) of 0.927 ± 0.044 and balanced accuracy (BACC) of 0.963 ± 0.022. These metrics surpassed those of the existing PeptideRanker model, which is widely used in bioactive peptide studies. Based on in silico screening, we identified and synthesized six novel PASAPs derived from tilapia collagen: KKHVWFGE, NGTPGAMGPR, PGAAGLKGDR, DGAPGPKGDR, TGPVGMPGAR, and GAPGGAGGVGEPGR. In vitro assays revealed that all six peptides exhibited significant inhibitory activity against aging-related enzymes, with the most pronounced effects on elastase and collagenase. A comprehensive analysis of the C-terminal amino acid residues indicated that the presence of arginine (R) at the C-terminus notably enhanced peptide binding to aging-related enzymes. This enhancement was attributed to an increased number of hydrogen bonds and stronger chemical interactions, which augmented the aging-related enzyme inhibitory activity of the peptides. In summary, this study proposed an effective strategy for discovering PASAPs from collagen and validated the machine learning model through experimental evidence. Structure–activity relationship insights can guide the synthesis of bioactive peptides and the selection of proteases for bioactive peptide production. [ABSTRACT FROM AUTHOR]
Copyright of Collagen & Leather is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Βάση Δεδομένων: Complementary Index
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  – Url: https://dx.doi.org/doi:10.1186/s42825-025-00215-8
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  Data: Discovering potential anti-skin-aging peptides in collagen: computer-assisted rapid screening and structure–activity relationships.
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  Data: <searchLink fieldCode="AR" term="%22Zhang%2C+Ruihao%22">Zhang, Ruihao</searchLink><br /><searchLink fieldCode="AR" term="%22Li%2C+Yang%22">Li, Yang</searchLink><br /><searchLink fieldCode="AR" term="%22Li%2C+Yonghui%22">Li, Yonghui</searchLink><br /><searchLink fieldCode="AR" term="%22Zhang%2C+Hui%22">Zhang, Hui</searchLink>
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  Data: Collagen & Leather; 9/1/2025, Vol. 7 Issue 1, p1-20, 20p
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  Data: <searchLink fieldCode="DE" term="%22Skin+aging%22">Skin aging</searchLink><br /><searchLink fieldCode="DE" term="%22Peptides%22">Peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Enzyme+inhibitors%22">Enzyme inhibitors</searchLink><br /><searchLink fieldCode="DE" term="%22Structure-activity+relationships%22">Structure-activity relationships</searchLink><br /><searchLink fieldCode="DE" term="%22Collagen%22">Collagen</searchLink><br /><searchLink fieldCode="DE" term="%22Data+analysis%22">Data analysis</searchLink><br /><searchLink fieldCode="DE" term="%22Dietary+bioactive+peptides%22">Dietary bioactive peptides</searchLink><br /><searchLink fieldCode="DE" term="%22Machine+learning%22">Machine learning</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The application of peptides as inhibitors of skin aging is a promising area of research. Previous researches have predominantly focused on extracting anti-aging peptides from the collagen of specific animals, while large-scale rapid screening and analysis of the structure–activity relationships of these peptides have been scarcely reported. In the present investigation, we developed a machine learning model for screening potential anti-skin-aging peptides (PASAPs), achieving a Matthews correlation coefficient (MCC) of 0.927 ± 0.044 and balanced accuracy (BACC) of 0.963 ± 0.022. These metrics surpassed those of the existing PeptideRanker model, which is widely used in bioactive peptide studies. Based on in silico screening, we identified and synthesized six novel PASAPs derived from tilapia collagen: KKHVWFGE, NGTPGAMGPR, PGAAGLKGDR, DGAPGPKGDR, TGPVGMPGAR, and GAPGGAGGVGEPGR. In vitro assays revealed that all six peptides exhibited significant inhibitory activity against aging-related enzymes, with the most pronounced effects on elastase and collagenase. A comprehensive analysis of the C-terminal amino acid residues indicated that the presence of arginine (R) at the C-terminus notably enhanced peptide binding to aging-related enzymes. This enhancement was attributed to an increased number of hydrogen bonds and stronger chemical interactions, which augmented the aging-related enzyme inhibitory activity of the peptides. In summary, this study proposed an effective strategy for discovering PASAPs from collagen and validated the machine learning model through experimental evidence. Structure–activity relationship insights can guide the synthesis of bioactive peptides and the selection of proteases for bioactive peptide production. [ABSTRACT FROM AUTHOR]
– Name: Abstract
  Label:
  Group: Ab
  Data: <i>Copyright of Collagen & Leather is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1186/s42825-025-00215-8
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        Text: English
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              M: 09
              Text: 9/1/2025
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              Y: 2025
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