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Studies On Prebiotic Synthesis Of The Functional Peptide And Its Derivative Induced By Phosphorous

Posted on:2019-09-15Degree:MasterType:Thesis
Country:ChinaCandidate:W Y ShuFull Text:PDF
GTID:2370330545997456Subject:Chemical Biology
Abstract/Summary:PDF Full Text Request
The Ser-His dipeptide is one of the smallest active peptides,which is currently reported to have a variety of enzyme activities,is considered to be the embryonic evolution of modern proteolytic enzymes.In order to study the properties of phosphorus on life matter,especially bioactive peptides and their derivatives in the primeval environment,this paper takes Ser as the core amino acid,discusses the reactivity of serine and other amino acids in the activation of organic phosphorus and inorganic phosphorus reagent,and the feasibility of obtaining the precursor of glycerol phosphatidylcholine containing serine structure.Specifically,the following three aspects of the work are mainly carried out:Firstly,N-DIPP-Ser and His can selectively form Ser-His dipeptides in the aqueous phase than other ancient amino acids,such as Ala,Ser,Pro and Asp,with a yield of about 27%.This means that the Ser-His can be obtained spontaneously and competitively on the early earth under the activation of phosphorus,a finding that further suggests that Ser-His may be a potential candidate for the evolution of modern proteolytic enzymes.Secondly,to try construct membrane-peptide system with the aqueous phase reaction of Pam,Ser and His,it is possible to construct the vesicles from oleic acid at prebiotic condition to investigate the feasibility of obtaining Ser-His induced by inorganic phosphorus and the effect of the vesicle micro-reactor on the peptide formation.The results showed that Ser and His could form Ser-His at the yield of 2.5%with the activation of inorganic phosphate P3m.However,due to the efficiency of phosphorylation of amino acids and formation of peptide,the yield ratio of Ser-His and His-Ser was 1:6 and the homo-dipeptide is less than hetero-dipeptide.This finding is proving to be more powerful evidence that the way of amino acid phosphorylation affects the peptide sequence with selectivity,which is of great significance for the effective production of active small peptides.Besides,it was found that the presence of oleic acid did not obviously promote the production of Ser-His dipeptide.Thirdly,a ternary reaction system of P3m,serine and glycerol were used to study the membrane construction of the glycerol-phospholipid serine.It was first discovered by the control experiment that serine was introduced into the binary system of P3m and glycerol reaction,and the type of glycerol phosphate was increased from one to five.It can be explained that P-N intermediates(phosphorylated serine)make it easier to react with glycerol,so it can be inferred that N-phosphorylated amino acids play an important role in the molecular mechanism of biofilm evolution.At the same time,it provides a favorable evidence for the construction of the nucleic acid-protein-membrane co-origin model.
Keywords/Search Tags:Prebiotic chemistry, N-phosphoryl amino acid, Ser-his, Selectivity
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