Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling

Liu, Yan; Shi, Yanhong; Liu, Xiaoxia; Lin, MingKun; Lin, Donghai; Zhao, Yufen

doi:10.1007/s11426-010-3192-z

Cited by 2 publications

(1 citation statement)

References 32 publications

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“…The most obvious postulate is that it is a minimalistic analogue of serine hydrolases [ 21 ]. The group of YuFen Zhao, who first reported the Ser-His activity, has followed with a number of studies on hydrolytic activity, analytics and modeling of this interesting dipeptide [ 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 ]. However, none of those studies have actually tried to elucidate in detail the mechanism by which Ser-His hydrolysis functions.…”

Section: Seryl-histidine Catalyzes the Formation Of Peptide Bonds mentioning

confidence: 99%

Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine

Wieczorek

Adamala

Gasperi

et al. 2017

Life

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Catalysis is an essential feature of living systems biochemistry, and probably, it played a key role in primordial times, helping to produce more complex molecules from simple ones. However, enzymes, the biocatalysts par excellence, were not available in such an ancient context, and so, instead, small molecule catalysis (organocatalysis) may have occurred. The best candidates for the role of primitive organocatalysts are amino acids and short random peptides, which are believed to have been available in an early period on Earth. In this review, we discuss the occurrence of primordial organocatalysts in the form of peptides, in particular commenting on reports about seryl-histidine dipeptide, which have recently been investigated. Starting from this specific case, we also mention a peptide fragment condensation scenario, as well as other potential roles of peptides in primordial times. The review actually aims to stimulate further investigation on an unexplored field of research, namely one that specifically looks at the catalytic activity of small random peptides with respect to reactions relevant to prebiotic chemistry and early chemical evolution.

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Section: Seryl-histidine Catalyzes the Formation Of Peptide Bonds mentioning

confidence: 99%

Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine

Wieczorek

Adamala

Gasperi

et al. 2017

Life

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Evolutionary relationships between seryl-histidine dipeptide and modern serine proteases from the analysis based on mass spectrometry and bioinformatics

Liu

Gao

et al. 2017

Amino Acids

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Seryl-histidine dipeptide (Ser-His) has been recognized as the shortest peptide with hydrolysis cleavage activity; however, its protein cleavage spectrum has not yet been fully explored. Here, four differently folded proteins were treated with Ser-His, and the digestion products were evaluated with high-resolution mass spectrometry. The cleavage efficiency and cleavage propensity of Ser-His against these protein substrates were calculated at both the primary and secondary sequence levels. The above experiments show that Ser-His cleaves a broad spectrum of substrate proteins of varying secondary structures. Moreover, Ser-His could cleave at all 20 amino acids with different efficiencies according to the protein, which means that Ser-His has the original digestion function of serine proteases. Furthermore, we collected and compared the catalytic sites and cleavage sites of 340 extant serine proteases derived from 17 representative organisms. A consensus motif Ser-[X]-His was identified as the major pattern at the catalytic sites of serine proteases from all of the organisms represented except Danio rerio, which uses Ser-Lys instead. This finding indicates that Ser-His is the core component of the serine protease catalytic site. Moreover, our analysis revealed that the cleavage sites of modern serine proteases have become more specific over the evolutionary history of this family. Based on the above analysis results, it could be found that Ser-His is likely the original serine protease and maybe the evolutionary core of modern serine proteases.

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Evaluation of non-covalent interaction between Seryl-Histidine dipeptide and cyclophilin A using NMR and molecular modeling

Cited by 2 publications

References 32 publications

Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine

Small and Random Peptides: An Unexplored Reservoir of Potentially Functional Primitive Organocatalysts. The Case of Seryl-Histidine

Evolutionary relationships between seryl-histidine dipeptide and modern serine proteases from the analysis based on mass spectrometry and bioinformatics

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