内源性和外源性 L-氨基酸及其衍生物在水溶液和混合溶液中的质子常数:揭开分子的秘密

IF 7.2 2区 生物学 Q1 BIOPHYSICS Quarterly Reviews of Biophysics Pub Date : 2024-10-18 DOI:10.1017/S0033583524000118
Marek Pająk, Jakub Fichna, Magdalena Woźniczka
{"title":"内源性和外源性 L-氨基酸及其衍生物在水溶液和混合溶液中的质子常数:揭开分子的秘密","authors":"Marek Pająk, Jakub Fichna, Magdalena Woźniczka","doi":"10.1017/S0033583524000118","DOIUrl":null,"url":null,"abstract":"<p><p>The aim of this review is to summarize the progress made in the determination of the protonation constants of biologically active ligands: endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solutions using different experimental techniques. The knowledge of the protonation constants of the aforementioned ligands is crucial for the determination of the equilibrium constants of complex formation and thus for the understanding of complex biological reactions such as transamination, racemization, and decarboxylation. Thus, the protonation constants of ligands are a measure of their ability to form complexes with metal ions. This knowledge not only helps to understand fundamental biochemical processes, but also has practical applications in areas such as drug design, where ligands are often targeted for therapeutic purposes. The activity of the ligands tends to increase after complexation and their order is consistent with the values of the stepwise dissociation constants of the complexes formed. Understanding the properties of ligands by determining their protonation constants in different environments and their interactions with surrounding molecules is crucial to unraveling the complexity of biological systems.</p>","PeriodicalId":20828,"journal":{"name":"Quarterly Reviews of Biophysics","volume":"57 ","pages":"e10"},"PeriodicalIF":7.2000,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Protonation constants of endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solution: Unraveling molecular secrets.\",\"authors\":\"Marek Pająk, Jakub Fichna, Magdalena Woźniczka\",\"doi\":\"10.1017/S0033583524000118\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The aim of this review is to summarize the progress made in the determination of the protonation constants of biologically active ligands: endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solutions using different experimental techniques. The knowledge of the protonation constants of the aforementioned ligands is crucial for the determination of the equilibrium constants of complex formation and thus for the understanding of complex biological reactions such as transamination, racemization, and decarboxylation. Thus, the protonation constants of ligands are a measure of their ability to form complexes with metal ions. This knowledge not only helps to understand fundamental biochemical processes, but also has practical applications in areas such as drug design, where ligands are often targeted for therapeutic purposes. The activity of the ligands tends to increase after complexation and their order is consistent with the values of the stepwise dissociation constants of the complexes formed. Understanding the properties of ligands by determining their protonation constants in different environments and their interactions with surrounding molecules is crucial to unraveling the complexity of biological systems.</p>\",\"PeriodicalId\":20828,\"journal\":{\"name\":\"Quarterly Reviews of Biophysics\",\"volume\":\"57 \",\"pages\":\"e10\"},\"PeriodicalIF\":7.2000,\"publicationDate\":\"2024-10-18\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Quarterly Reviews of Biophysics\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1017/S0033583524000118\",\"RegionNum\":2,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOPHYSICS\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Quarterly Reviews of Biophysics","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1017/S0033583524000118","RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOPHYSICS","Score":null,"Total":0}
引用次数: 0

摘要

本综述旨在总结利用不同实验技术测定生物活性配体(内源和外源 L-氨基酸及其衍生物)在水溶液和混合溶液中的质子常数方面所取得的进展。了解上述配体的质子化常数对于确定络合物形成的平衡常数,进而了解转氨、消旋化和脱羧等复杂的生物反应至关重要。因此,配体的质子化常数是衡量配体与金属离子形成络合物能力的标准。这些知识不仅有助于了解基本的生物化学过程,而且在药物设计等领域也有实际应用,因为配体通常是治疗目的的靶标。配体的活性在络合后呈上升趋势,其顺序与所形成络合物的分步解离常数值一致。通过测定配体在不同环境中的质子化常数及其与周围分子的相互作用来了解配体的特性,对于揭示生物系统的复杂性至关重要。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Protonation constants of endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solution: Unraveling molecular secrets.

The aim of this review is to summarize the progress made in the determination of the protonation constants of biologically active ligands: endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solutions using different experimental techniques. The knowledge of the protonation constants of the aforementioned ligands is crucial for the determination of the equilibrium constants of complex formation and thus for the understanding of complex biological reactions such as transamination, racemization, and decarboxylation. Thus, the protonation constants of ligands are a measure of their ability to form complexes with metal ions. This knowledge not only helps to understand fundamental biochemical processes, but also has practical applications in areas such as drug design, where ligands are often targeted for therapeutic purposes. The activity of the ligands tends to increase after complexation and their order is consistent with the values of the stepwise dissociation constants of the complexes formed. Understanding the properties of ligands by determining their protonation constants in different environments and their interactions with surrounding molecules is crucial to unraveling the complexity of biological systems.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Quarterly Reviews of Biophysics
Quarterly Reviews of Biophysics 生物-生物物理
CiteScore
12.90
自引率
1.60%
发文量
16
期刊介绍: Quarterly Reviews of Biophysics covers the field of experimental and computational biophysics. Experimental biophysics span across different physics-based measurements such as optical microscopy, super-resolution imaging, electron microscopy, X-ray and neutron diffraction, spectroscopy, calorimetry, thermodynamics and their integrated uses. Computational biophysics includes theory, simulations, bioinformatics and system analysis. These biophysical methodologies are used to discover the structure, function and physiology of biological systems in varying complexities from cells, organelles, membranes, protein-nucleic acid complexes, molecular machines to molecules. The majority of reviews published are invited from authors who have made significant contributions to the field, who give critical, readable and sometimes controversial accounts of recent progress and problems in their specialty. The journal has long-standing, worldwide reputation, demonstrated by its high ranking in the ISI Science Citation Index, as a forum for general and specialized communication between biophysicists working in different areas. Thematic issues are occasionally published.
期刊最新文献
Review of contemporary fluorescence correlation spectroscopy method in diverse solution studies. Optical scattering methods for the label-free analysis of single biomolecules. The development and applications of multidimensional biomolecular spectroscopy illustrated by photosynthetic light harvesting. Protonation constants of endo- and exogenous L-amino acids and their derivatives in aqueous and mixed solution: Unraveling molecular secrets. Solution-based biophysical characterization of conformation change in structure-switching aptamers.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1