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Titlebook: Collagen Mimetic Peptides and Their Biophysical Characterization; Jianxi Xiao Book 2024 Springer Nature Singapore Pte Ltd. 2024 Biomimetic

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发表于 2025-3-21 16:32:00 | 显示全部楼层 |阅读模式
书目名称Collagen Mimetic Peptides and Their Biophysical Characterization
编辑Jianxi Xiao
视频videohttp://file.papertrans.cn/243/242200/242200.mp4
概述Addresses every important aspect of collagen mimic peptides.Introduces the latest studies on both homotrimeric and heterotrimeric collagen peptides.Provides protocols for studying thermal stability, s
丛书名称Springer Series in Biomaterials Science and Engineering
图书封面Titlebook: Collagen Mimetic Peptides and Their Biophysical Characterization; Jianxi Xiao Book 2024 Springer Nature Singapore Pte Ltd. 2024 Biomimetic
描述.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
出版日期Book 2024
关键词Biomimetic peptide; Triple helix; Collagen; Protein structure; Protein dynamics; Biophysics characterizat
版次1
doihttps://doi.org/10.1007/978-981-10-1941-8
isbn_softcover978-981-97-7669-6
isbn_ebook978-981-10-1941-8Series ISSN 2195-0644 Series E-ISSN 2195-0652
issn_series 2195-0644
copyrightSpringer Nature Singapore Pte Ltd. 2024
The information of publication is updating

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Hierarchical Structure of Collagen,equence, enriched with glycine, proline, and hydroxyproline, crucial for maintaining the stability of its triple helix conformation. The secondary structure features a left-handed polyproline II (PPII) helix, resulting from the repetitive sequence and restricted rotation around proline and hydroxypr
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Synthesis of Collagen Mimetic Peptides,icate hierarchical arrangement. To surmount these obstacles, collagen mimetic peptides, comprising repetitive (Gly-X-Y). sequences, have emerged as invaluable tools for probing the sequential and structural fundamentals of collagen‘s functionality and pathogenesis. This chapter is dedicated to eluci
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Conformational and Dynamic Characterization of Collagen Mimic Peptides by NMR Spectroscopy,cule‘s considerable size and rod-like configuration. To overcome this challenge, .N/.C-isotopically selectively labeled triple helical peptides have been constructed to elucidate collagen‘s structural and functional intricacies. This chapter provides an in-depth examination of NMR techniques tailore
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Fluorescence Detection of Collagen Peptides,and highly sensitive optical technique reliant on fluorophore emission, enables precise biomolecule quantification. This chapter offers a comprehensive overview of customized fluorescence assays for collagen peptides, notably focusing on fluorescence self-quenching assays. These assays detect change
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Collagen Mimetic Peptides for Targeting Pathological Collagen,athological collagen for diagnosis and prognosis. Innovative collagen mimetic peptides selectively bind to denatured collagen, promoting triple helix refolding by interacting with its unfolded chains, demonstrating high specificity for pathological collagen. This chapter explores the development of
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