气候变化领域集成服务门户(CCPortal): Selective incorporation of proteinaceous over nonproteinaceous cationic amino acids in model prebiotic oligomerization reactions

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DOI	10.1073/pnas.1904849116
	Selective incorporation of proteinaceous over nonproteinaceous cationic amino acids in model prebiotic oligomerization reactions
	Frenkel-Pinter M.; Haynes J.W.; Martin C.; Petrov A.S.; Burcar B.T.; Krishnamurthy R.; Hud N.V.; Leman L.J.; Williams L.D.
发表日期	2019
ISSN	0027-8424
起始页码	16338
结束页码	16346
卷号	116 期号:33
英文摘要	Numerous long-standing questions in origins-of-life research center on the history of biopolymers. For example, how and why did nature select the polypeptide backbone and proteinaceous side chains? Depsipeptides, containing both ester and amide linkages, have been proposed as ancestors of polypeptides. In this paper, we investigate cationic depsipeptides that form under mild dry-down reactions. We compare the oligomerization of various cationic amino acids, including the cationic proteinaceous amino acids (lysine, Lys; arginine, Arg; and histidine, His), along with nonproteinaceous analogs of Lys harboring fewer methylene groups in their side chains. These analogs, which have been discussed as potential prebiotic alternatives to Lys, are ornithine, 2,4-diaminobu-tyric acid, and 2,3-diaminopropionic acid (Orn, Dab, and Dpr). We observe that the proteinaceous amino acids condense more extensively than these nonproteinaceous amino acids. Orn and Dab readily cyclize into lactams, while Dab and Dpr condense less efficiently. Furthermore, the proteinaceous amino acids exhibit more selective oligomerization through their α-amines relative to their side-chain groups. This selectivity results in predominantly linear depsipeptides in which the amino acids are α-amine−linked, analogous to today’s proteins. These results suggest a chemical basis for the selection of Lys, Arg, and His over other cationic amino acids for incorporation into proto-proteins on the early Earth. Given that electrostatics are key elements of protein−RNA and protein−DNA interactions in extant life, we hypothesize that cationic side chains incorporated into proto-peptides, as reported in this study, served in a variety of functions with ancestral nucleic acid polymers in the early stages of life. © 2019 National Academy of Sciences. All rights reserved.
英文关键词	Chemical evolution; Condensation dehydration; Depsipeptides; Peptide evolution; Prebiotic chemistry
语种	英语
scopus关键词	2,3 diaminopropionic acid; 2,4 diaminobutyric acid; amino acid; arginine; carbene; depsipeptide; histidine; hydroxyacid; lactam; lysine; ornithine; polymer; prebiotic agent; 2,3-diaminopropionic acid; 2,4-diaminobutyric acid; amino acid; aminobutyric acid derivative; beta alanine; cation; DNA binding protein; peptide; protein; RNA binding protein; amino acid analysis; Article; chemical structure; controlled study; cross linking; cyclization; molecular interaction; oligomerization; polymerization; priority journal; protein analysis; protein DNA binding; protein RNA binding; proton nuclear magnetic resonance; static electricity; symbiosis; biogenesis; chemistry; genetics; Amino Acids; Aminobutyrates; beta-Alanine; Cations; Depsipeptides; DNA-Binding Proteins; Origin of Life; Peptides; Proteins; RNA-Binding Proteins; Static Electricity
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/158963
作者单位	Frenkel-Pinter, M., National Science Foundation (NSF), National Aeronautics and Space Administration (NASA) Center for Chemical Evolution, Atlanta, GA 30332, United States, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, United States, NASA Center for the Origins of Life, Georgia Institute of Technology, Atlanta, GA 30332, United States; Haynes, J.W., National Science Foundation (NSF), National Aeronautics and Space Administration (NASA) Center for Chemical Evolution, Atlanta, GA 30332, United States, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, United States; Martin, C., National Science Foundation (NSF), National Aeronautics and Space Administration (NASA) Center for Chemical Evolution, Atlanta, GA 30332, United States, School of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA 30332, United States; Petrov, A.S., National Science Foundation (NSF), National Aeronautics and Space Administr...
推荐引用方式 GB/T 7714	Frenkel-Pinter M.,Haynes J.W.,Martin C.,et al. Selective incorporation of proteinaceous over nonproteinaceous cationic amino acids in model prebiotic oligomerization reactions[J],2019,116(33).
APA	Frenkel-Pinter M..,Haynes J.W..,Martin C..,Petrov A.S..,Burcar B.T..,...&Williams L.D..(2019).Selective incorporation of proteinaceous over nonproteinaceous cationic amino acids in model prebiotic oligomerization reactions.Proceedings of the National Academy of Sciences of the United States of America,116(33).
MLA	Frenkel-Pinter M.,et al."Selective incorporation of proteinaceous over nonproteinaceous cationic amino acids in model prebiotic oligomerization reactions".Proceedings of the National Academy of Sciences of the United States of America 116.33(2019).