Non-Covalent Modification of Collagen Scaffolds

描述（由申请人提供）：胶原蛋白用于各种医疗应用，从止血材料和生物相容性涂层到药物输送和组织工程。传统上，胶原蛋白被用作被动（但具有生物相容性）的材料，保护受伤部位并支持愈合过程。今天，人们对胶原蛋白作为生物活性支架重新产生了兴趣，它可以为特定组织的形成提供理想的环境。这引起了人们对将生物活性成分（如生长因子、抗菌剂或细胞排斥剂）固定在天然胶原蛋白上的广泛兴趣。在本研究中，我们希望研究模拟胶原肽（CMP）及其衍生物在胶原支架上的非化学固定，并探索其作为微血管工程目标的新型胶原修饰技术的潜力。

DESCRIPTION (provided by applicant): Collagen is used in a variety of medical applications ranging from hemostatic materials and biocompatible coatings to drug delivery and tissue engineering. Traditionally, collagen is used as passive (but biocompatible) materials that protect injured sites and support healing processes. Today, there is a renewed interest in collagen as bioactive scaffolds that can provide ideal environment for specific tissue formation. This has led to widespread interests in immobilizing bioactive components (such as growth factors, antimicrobial agents, or cell-repellent) to natural collagen. In this proposal we wish to investigate nonchemical immobilization of collagen mimetic peptides (CMP) and CMP derivatives on collagen scaffolds, and explore its potential as a new collagen modification technique targeted for microvasculature engineering. Collagen mimetic peptides (CMPs) are peptides, typically of less than 30 amino acids, composed of multimers of known helicogenic trimers (e.g. ProHypGly). They have been highly useful in determining the structure and stability of natural collagens and their collagen-like triple helical structure and reversible association (melting) behaviors are documented in the literatures. In our previous studies, we discovered that CMPs can bind to collagen films (type I) under controlled thermal condition. Main goals of this research are to further understand the CMP-collagen interaction, identify optimal CMP structure that exhibit efficient and reversible binding to collagen under physiological or near-physiological condition, and demonstrate the practical use of the poly(ethyleneglycol)-CMP conjugate in controlling the endothelial cell (ED) organization in 2D and 3D collagen scaffolds. In the long run, we wish to develop this approach into a more general collagen modification method that can provide novel solutions to complications after vascular and ocular surgery and to add therapeutic activity to conventional collagen-based biomaterials (see support letter from The Wilmer Ophthalmological Institute of the Johns Hopkins Medical School).