Dipeptide seryl-histidine and related oligopeptides cleave DNA, protein, and a carboxyl ester

Li, Yunsheng; Zhao, Yufen; Hatfield, Scott; Wan, Rong; Zhu, Qin; Li, Xionghong; McMills, Mark C.; Ma, Yuan; Li, Jing; Brown, Kenneth L.; He, Chen; Liu, Fang; Chen, Xiaozhuo

doi:10.1016/s0968-0896(00)00208-x

Cited by 99 publications

(74 citation statements)

References 24 publications

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“…A number of approaches have emerged in the pursuit of a synthetic catalyst (Figure 2). These approaches seek to mimic multiple aspects of biocatalysis, including (a) use of properties of primary peptide sequence to control the immediate chemical environment and functionality [8]. To further enhance activity, the peptides may be engineered into a designed environment, for example: (b) presentation of reactive sites for catalysis on scaffolds and particles [18,19] (c) design of binding pockets for substrates or transition states.…”

Section: Design Approaches In the Pursuit Of Synthetic Catalystsmentioning

confidence: 99%

“…What they discovered is surprising, in that the dipeptide Ser-His has the capability to cleave amide and ester bonds. The group reported that on incubation with Ser-His, cleavage was observed with linear and circular DNAs, proteins (BSA) and carboxyl ester substrate p-nitrophenyl acetate (p-NPA) [8]. These processes occur over a wide range of physical and chemical conditions.…”

Section: Primary Sequence In Catalysismentioning

confidence: 99%

“…The fact that enzymes evolved suggests that simpler functional precursors to hydrolases may exist and these could provide information about the design of short peptide catalysts. Indeed, it has been observed that the dipeptide seryl-histidine (Ser-His) is able to catalyse a number of hydrolytic reactions in water [8], albeit with low selectivity and modest rates.…”

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confidence: 99%

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Short Peptides in Minimalistic Biocatalyst Design

Duncan

Ulijn

2015

Biocatalysis

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As an example, let's look at a common class of biocatalysts, proteases, which possess the ability to hydrolyse amide (as well as ester) bonds. This amide hydrolysis reaction is extremely challenging with a half-life of 450 years [9,10]. Protease enzymes make use of a catalytic triad (Figure 1a Abstract: We review recent developments in the use of short peptides in the design of minimalistic biocatalysts focusing on ester hydrolysis. A number of designed peptide nanostructures are shown to have (modest) catalytic activity. Five features are discussed and illustrated by literature examples, including primary peptide sequence, nanosurfaces/scaffolds, binding pockets, multivalency and the presence of metal ions. Some of these are derived from natural enzymes, but others, such as multivalency of active sites on designed nanofibers, may give rise to new features not found in natural enzymes. Remarkably, it is shown that each of these design features give rise to similar rate enhancements in ester hydrolysis. Overall, there has been significant progress in the development of fundamental understanding of the factors that influence binding and activity in recent years, holding promise for increasingly rational design of peptide based biocatalysts.

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Section: Design Approaches In the Pursuit Of Synthetic Catalystsmentioning

confidence: 99%

Section: Primary Sequence In Catalysismentioning

confidence: 99%

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confidence: 99%

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Short Peptides in Minimalistic Biocatalyst Design

Duncan

Ulijn

2015

Biocatalysis

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“…Amino acid polymerization should lead to short random peptide strands with sufficient structural complexity to show enzymatic (catalytic) activity, as low catalytic activity was established in even peptide dimers [64]. Polycondensation of amino acids is possible in solution when monomers are activated using N-carboxyanhydride [65][66][67][68], however sequence specificity is impossible in such a situation.…”

Section: Membranes As Multiphase Reaction Systems and Reaction Scaffoldsmentioning

confidence: 99%

Primitive Membrane Formation, Characteristics and Roles in the Emergent Properties of a Protocell

Maurer

Monnard

2011

Entropy

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All contemporary living cells are composed of a collection of self-assembled molecular elements that by themselves are non-living but through the creation of a network exhibit the emergent properties of self-maintenance, self-reproduction, and evolution. This short review deals with the on-going research that aims at either understanding how life emerged on the early Earth or creating artificial cells assembled from a collection of small chemicals. In particular, this article focuses on the work carried out to investigate how self-assembled compartments, such as amphiphile and lipid vesicles, contribute to the emergent properties as part of a greater system.

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“…The hydrolysis is realized by the unique collaboration between Histidine-57 (His-57), and Aspartate-102 (Asp-102) [5]. Intrigued by this performance, several groups have tried to construct model systems with hydrolytic activity and different peptide based systems have been developed in this context [6][7][8][9][10][11][12][13][14][15][16]. We must bear in mind that stable secondary structures such as helices only become important for rather long sequences of polypeptides.…”

Section: Introductionmentioning

confidence: 99%