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Exploring the structural requirements of collagen-binding peptides.

ABSTRACT: Collagen synthesis and tissue remodeling are involved in many diseases; therefore, collagen-specific binding agents have been developed to study collagen changes in various tissues. Based on a recently reported collagen binding peptide, which contains unnatural biphenylalanine (Bip) amino acid residue, constructs with various structure variations were synthesized to explore the contributions of unnatural Bip residue, conformational restrain, and amino acid sequence in collagen recognition. Their binding efficiency to collagens was evaluated in vitro using pure collagens. The results indicate that the C-terminal unnatural Bip residue, rather than the peptide sequence or conformational restrain, dominated the collagen I binding. Subsequent tissue binding study showed that the selected peptide did not offer preferential selectivity over collagen I in tissue, suggesting that a simple in vitro binding assay cannot adequately model the complex biological environment.

SUBMITTER: Abd-Elgaliel WR

PROVIDER: S-EPMC3637416 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Exploring the structural requirements of collagen-binding peptides.

Abd-Elgaliel Wael R WR Tung Ching-Hsuan CH

Biopolymers 20130401 2

Collagen synthesis and tissue remodeling are involved in many diseases; therefore, collagen-specific binding agents have been developed to study collagen changes in various tissues. Based on a recently reported collagen binding peptide, which contains unnatural biphenylalanine (Bip) amino acid residue, constructs with various structure variations were synthesized to explore the contributions of unnatural Bip residue, conformational restrain, and amino acid sequence in collagen recognition. Their ...[more]

PMID: 23436394

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Project description:OBJECTIVES:The aim of the study is to evaluate the pharmacokinetics and microbiodistribution of Cu-labeled collagen-binding peptides. METHODS:The affinity constant (KD), association (ka), and dissociation rate constant (kd) for the peptide collagelin or its analog (named CRPA) binding to collagen were measured by biolayer interferometric analysis. Rats (n=4-5) with myocardial infarction or normal were injected intravenously with the Cu-labeled peptides or Cu-DOTA as a control. Dynamic PET imaging was performed for 60?min at 7-8 weeks after infarct. Fluorine-18 fluorodeoxyglucose PET imaging was performed to identify the viable myocardium. To validate the PET images, slices of heart samples from the base to the apex were analyzed using autoradiography and histology. RESULT:The peptides bound to collagen with a KD of ?0.9?µmol/l. The Cu-peptides and Cu-DOTA accumulated in the infarct area (confirmed by autoradiography and histology images) within 1?min of injection and were excreted rapidly through the renal system. The blood clearance curves were biphasic with elimination half-lives of 21.9±2.4, 26.2±4.6, and 21.2±2.1?min for Cu-CRPA, Cu-collagelin, and the control Cu-DOTA, respectively. The clearance half-lives from the focal fibrotic tissue (24.1±1.5, 25.6±8.0, and 21.4±1.3?min, respectively) and remote myocardium (20.8±0.7, 21.0±5.5, and 19.1±2.4?min, respectively) were not significantly different. The uptake ratios of infarct-to-remote myocardium (1.93±0.18, 2.15±0.38, and 1.88±0.08, respectively) for Cu-CRPA, Cu-collagelin, and Cu-DOTA remained stable for the time period between 10 and 60?min. CONCLUSION:The distribution of the Cu-collagelin probes corresponds to the heterogeneous distribution of expanded extracellular space in the setting of myocardial infarction. The overall washout rate from the fibrous tissue was determined by the slow washout rate (t1/2?20?min) of the peptides from the extracellular space to the vasculature, not by the dissociation rate (t1/2<2?min) of the Cu-peptides from collagen.

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Exploring the structural requirements of collagen-binding peptides.

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Exploring the structural requirements of collagen-binding peptides.

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