Cleavage of BSA by a dipeptide seryl-histidine

Chen, Jing; Wan, Rong; Liu, Hai; Cheng, Changmei; Zhao, Yufen

doi:10.1007/bf02443596

Cited by 7 publications

(8 citation statements)

References 23 publications

(10 reference statements)

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“…Our previous work [8][9][10][11] showed that Ser-His could cleave BSA and GFP. The optimal temperature for Ser-His cleaving protein is 50 °C [8].…”

Section: Experiments Of Ser-his Cleaving Cypamentioning

confidence: 99%

“…In our previous work, we reported that Seryl-Histidine dipeptide (Ser-His) possesses interesting properties [7][8][9][10][11]. It could not only cleave DNA and carboxyl esters by a hydrolysis mechanism [7,8], but also cleave bovine serum albumen (BSA) [8][9][10] and green fluorescence protein (GFP) [11] in a wide range of pH and temperature.…”

Section: Introductionmentioning

confidence: 99%

“…It could not only cleave DNA and carboxyl esters by a hydrolysis mechanism [7,8], but also cleave bovine serum albumen (BSA) [8][9][10] and green fluorescence protein (GFP) [11] in a wide range of pH and temperature. Therefore, as a protease mimics, Ser-His is attracting increasingly more attention for its special biological function [12,13].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2010

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Seryl-Histidine dipeptide (Ser-His) has been previously reported to be capable of cleaving DNAs and carboxyl esters, as well as proteins. The protein cleavage mechanism has not been addressed yet. As an initial step of protein cleavage activity, the non-covalent binding affinity of Ser-His for proteins is a crucial prerequisite. In this work, we took cyclophilin A (CyPA) as a substrate protein, and evaluated the non-covalent interaction between CyPA and Ser-His using a combination of NMR spectroscopy and molecular modeling approach. Two independent Ser-His binding sites on CyPA were detected using N-15-H-1 heteronuclear single-quantum coherence (HSQC) spectra. Each binding site binds one Ser-His molecule. Dissociation constants, K (d1) and K (d2), were estimated to be 2.07 and 6.66 mmol/L, respectively, indicative of the weak non-covalent interaction between Ser-His and CyPA. Based on molecular modeling results, we suggest that both the alpha-amino and the side chain hydroxyl group of Ser-His are crucial for the non-covalent interaction between Ser-His and CyPA. This work sheds light on the molecular mechanism of Ser-His and its analogues cleaving proteins.National Natural Science Foundation of China [20732004, 30730026, 20805037]; Ministry of Science and Technology of China [2007CB914304

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“…Our previous work [8][9][10][11] showed that Ser-His could cleave BSA and GFP. The optimal temperature for Ser-His cleaving protein is 50 °C [8].…”

Section: Experiments Of Ser-his Cleaving Cypamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2010

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“…[8][9][10][11][12][13] These compounds are cytotoxic, often correlated to the reductive cleavage of the azo bond which could be utilized for antimicrobial activity if they do not adversely affect the host. [14][15][16][17][18] Hence, materials for preparing azo compounds for a specific cause have to be chosen judiciously so that the product is an effective antimicrobial agent but not toxic to the host.…”

Section: Introductionmentioning

confidence: 99%

Synthesis, characterization, photo physical properties of two isomeric forms of an azo dye supported by DFT calculations and their interaction with DNA

et al. 2016

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A new azo compound 2‐(2‐hydroxyphenylazo)‐indole‐3/‐acetic acid was synthesized. It is a yellow solid when freshly prepared but upon exposure to light turns red gradually. The change in color may be controlled by lowering the temperature or by keeping the compound in the dark. IR and mass spectroscopy of the two forms are similar while UV‐vis, NMR and HPLC are different suggesting isomerization. Fluorescence emission of the yellow compound at 370 nm following excitation at 280 nm is different from the red showing emission at 460 nm upon excitation at 350 nm. Spectroscopy and fluorescence lifetime data suggest change from the yellow form to red is reversible. DFT calculations show the yellow and red forms to be the torsional rotamer and the trans isomer respectively.The cis isomer was determined theoreticallybut could not be isolated.The trans is stable than the cis by 18.825 kcal mol−1.Interaction of the isomers with DNA was studied with the help of UV‐vis and fluorescence spectroscopy. Binding parameters suggest change in spatial orientation makes the trans compound a slightly better binder of DNA than the torsional rotamer.

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“…Py/Py recognises both A•T and T•A base pairs. [8][9][10][11] Our laboratory carried out many investigations on small peptides and found that seryl-histidine dipeptide and related oligopeptides can cleave DNA, protein and carboxyl ester, 12,13 which is the shortest peptide ever reported in cleavage agents.…”

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confidence: 99%