This book embarks on an enlightening journey through the molecular landscape of collagen mimic peptides, shedding light on their significance and potential. In the intricate realm of biomolecules, collagen's preeminence as the most abundant protein in the human body, forming the foundational scaffolding of tissues and organs, renders it a subject of profound scientific interest. It explores diverse facets related to collagen mimic peptides, spanning aspects such as bioinformatic analysis, synthetic strategies, pathological collagen targeting, and the construction of homotrimeric, heterotrimeric and self-assembled peptide models. Furthermore, it provides an exhaustive investigation into biophysical techniques, encompassing Circular Dichroism (CD), X-ray crystallography, Nuclear Magnetic Resonance (NMR), Fluorescence, and Raman spectroscopy, thereby empowering researchers to unravel the structural intricacies of these peptides. The book unravels the profound implications of collagen mimic peptides across a spectrum of scientific domains, including protein science, biomaterials, bioanalysis, and beyond. Its accessibility and insights cater not only to seasoned researchers but also to undergraduate and graduate students eager to delve into the complexities of this fundamental protein.

Collagens are one of the most abundant proteins found in body tissues and organs, endowing structural integrity, mechanical strength, and multiple biological functions. Destabilized collagen inside human body leads to various degenerative diseases (ex. osteoarthritis) and ageing. This has continued to motivate the design of synthetic peptides and bio-synthetic polypeptides to closely mimic the native collagens in terms of triple helix structure and stability, potential for higher order assembly, and biological properties. However, the widespread application of de novo collagens has been limited in part by the need for hydroxylated proline in the formation of stable triple helical structures. To address this continued need, a hydroxyproline-free, thermally stable collagen-mimetic peptide (CLP-Cys) was rationally designed via the incorporation of electrostatically stabilized amino acid triplets. CLP-Cys was synthesized via solid phase peptide synthesis. The formation and stability of the triple helical structure were indicated via circular dichroism (CD) experiments and confirmed via differential scanning calorimetry (DSC) results. CLP-Cys also self-assembled into nano-rods and micro-fibrils, as evidenced via a combination of dynamic light scattering and transmission electron microscopy. Given the high thermal stability and its propensity for higher-order assembly, CLP-Cys was further functionalized at both the ends with a thermally responsive polymer, poly(diethylene glycol methyl ether methacrylate), (PDEGMEMA) to synthesize a biohybrid triblock copolymer. The CD results indicated that the triple helical form is retained, the thermal unfolding is sustained and helix to coil transition is reversible in the triblock hybrid context. The LCST of PDEGMEMA homopolymer (26 °C) is increased (to 35 °C) upon conjugation to the hydrophilic collagen peptide domain. Further, a combination of static light scattering, Cryo-SEM, TEM and confocal microscopy elucidated that the collapse of the thermo-responsive polymer upon heating (to above the LCST) leads to the assembly of these hybrid materials as micrometer sized spheres. At 75 °C a morphological transformation from spheres to fibrils were observed. These studies provided unique perspectives about the impact of stimuli-responsive polymers and the triple-helix forming peptides on each other; and how temperature as a stimulus can be employed to sequentially guide the assembly. The development of self-assembling hybrid materials with multiple sensitivities to temperature would offer useful opportunities in the design of stimuli-responsive nano-materials. The CLP-Cys peptide sequence has been designed to incorporate biologically relevant amino acid triplets (GEKGER) and its positive impact was seen via recruitment of human mesenchymal stem cells (hMSCs) for adhesion, spreading and proliferation on CLP-Cys functionalized glass and hyaluronic acid based hydrogel surfaces. Therefore, the prospects of these materials in biomedical applications including wound healing and tissue engineering are promising.

During the past decade we have witnessed not only an increase in knowledge of the "traditional" biophysical problems, but also an understanding of the molecular basis of various biological phenomena. The principles and methods of biophysics now provide an underpin ning of all of the basic biosciences and are the rational language for discussion between scientists of different disciplines. The International School on Biophysics Supramolecular Structure and Function held in Dubrovnik in September 1984 had as its goal to provide comprehensive discussions on a large number of subjects both for younger scientists at the doctoral or postdoctoral level interested in the molecular nature of fundamental biological entities, and for experienced scientists wishing to gain a broader insight into molecular structures and functions. The topics discussed at the School were inter- and intramolecular interactions in biological systems, and the structure, organization, and function of biological macromolecules and supramolecular assemblies. A number of topics were centered around either a biological problem or a physical technique, sometimes giving an unbalanced view of the field under discussion. Some of the topics required previous knowledge of basic biophysical principles, which were then applied to gain greater insight into the molecular functions of diverse supramolecular systems. Although not all the lectures could be prepared for publication in this volume, I hope that it contains valuable up-to-date information on various aspects of the molecular basis of life.

“Have you tried peptides? Small proteins, the best in the land! Won’t you try peptides? Keep all your body processes in hand! For labor and lactation oxytocin you must buy! Enkephalin always gives a good runner’s high! So won’t you try peptides? Small proteins, the best in the land!” The above words [1], penned by Gary Gisselman to open Peptide Ångst: La Triviata, the opera which made its world premiere on July 1, 1999, also serve as a fitting charge to the th 16 American Peptide Symposium. This latest edition of a premier biennial series was held under the auspices of the American Peptide Society, June 26–July 1, 1999, at the Minneapolis Convention Center, Minneapolis,Minnesota, with the undersigned serving as Co-Chairs. The fortunate coincidence of the calendar allowed us to set as the theme “Peptides for the New Millennium”, and in our judgment, the approximately 1200 participants [2] who converged in the Twin Cities from academic and industrial institutions in 36 countries were treated to an exciting and stimulating conference that left most everyone with an enthusiastic vision for the future of our field. The present Proceedings volume should serve as a handy reference source and succinct snapshot of peptide science at essentially its century mark – the clock having started with the initial contributions of Emil Fischer and Th. Curtius.

Not only does this book provide a comprehensive review of current research advances in collagen structure and mechanics, it also explores this biological macromolecule’s many applications in biomaterials and tissue engineering. Readers gain an understanding of the structure and mechanical behavior of type I collagen and collagen-based tissues in vertebrates across all length scales, from the molecular (nano) to the organ (macro) level.