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Collagen hybridizing peptide information


Schematic of a CHP strand (labeled with an "X" tag) hybridizing to denatured collagen chains and forming a collagen triple helix. During disease progression, tissue development, or ageing, collagen can be extensively degraded by collagenolytic proteases, causing its triple helix to unfold at the physiological temperature due to reduced thermal stability. X may represent a biotin or fluorescent tag.

A collagen hybridizing peptide (CHP) is a synthetic peptide sequence with typically 6 to 10 repeating units of the Gly-Xaa-Yaa amino acid triplet, which mimics the hallmark sequence of natural collagens.[1][2] A CHP peptide usually possesses a high content of proline and hydroxyproline in the Xaa and Yaa positions, which confers it a strong propensity to form the collagen's unique triple helix conformation.[1][3] In the single-stranded (monomeric) status, the peptide can recognize denatured collagen strands in tissues by forming a hybridized triple helix with the collagen strands.[2] This occurs via the triple helical chain assembly and inter-chain hydrogen bonding, in a manner similar to primers binding to melted DNA strands during PCR.[4] The binding does not depend on a specific sequence or epitope on collagen, enabling CHPs to target denatured collagen chains of different types.[5][6]

  1. ^ a b Shoulders, Matthew D.; Raines, Ronald T. (2009). "Collagen structure and stability". Annual Review of Biochemistry. 78: 929–958. doi:10.1146/annurev.biochem.77.032207.120833. ISSN 1545-4509. PMC 2846778. PMID 19344236.
  2. ^ a b Wahyudi, Hendra; Reynolds, Amanda A.; Li, Yang; Owen, Shawn C.; Yu, S. Michael (October 2016). "Targeting collagen for diagnostic imaging and therapeutic delivery". Journal of Controlled Release. 240: 323–331. doi:10.1016/j.jconrel.2016.01.007. PMC 4936964. PMID 26773768.
  3. ^ Persikov, A. V.; Ramshaw, J. A.; Kirkpatrick, A.; Brodsky, B. (2000-12-05). "Amino acid propensities for the collagen triple-helix". Biochemistry. 39 (48): 14960–14967. doi:10.1021/bi001560d. ISSN 0006-2960. PMID 11101312.
  4. ^ Li, Yang; Yu, S. Michael (December 2013). "Targeting and mimicking collagens via triple helical peptide assembly". Current Opinion in Chemical Biology. 17 (6): 968–975. doi:10.1016/j.cbpa.2013.10.018. ISSN 1879-0402. PMC 3863647. PMID 24210894.
  5. ^ Hwang, Jeongmin; Huang, Yufeng; Burwell, Timothy J.; Peterson, Norman C.; Connor, Jane; Weiss, Stephen J.; Yu, S. Michael; Li, Yang (2017-10-24). "In Situ Imaging of Tissue Remodeling with Collagen Hybridizing Peptides". ACS Nano. 11 (10): 9825–9835. doi:10.1021/acsnano.7b03150. ISSN 1936-0851. PMC 5656977. PMID 28877431.
  6. ^ Li, Yang; Ho, Daniel; Meng, Huan; Chan, Tania R.; An, Bo; Yu, Hanry; Brodsky, Barbara; Jun, Albert S.; Michael Yu, S. (2013-01-16). "Direct Detection of Collagenous Proteins by Fluorescently Labeled Collagen Mimetic Peptides". Bioconjugate Chemistry. 24 (1): 9–16. doi:10.1021/bc3005842. ISSN 1043-1802. PMC 3586774. PMID 23253177.

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