Bovine serum albumin with glycated carboxyl groups shows membrane-perturbing activities

Yang, Shin-Yi; Chen, Ying-Jung; Kao, Pei-Hsiu; Chang, Long‐Sen

doi:10.1016/j.abb.2014.10.001

Cited by 9 publications

(6 citation statements)

References 41 publications

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“…Albumin incorporation into liposome-DNA complexes enhanced transfection rates significantly (86,87), probably due to the membrane-permeabilizing effect of albumin. The disruption of bacterial membrane integrity could be visualized by microscopy (88,89).…”

Section: Albumin and ␣ 1 -Acidic-glycoproteinmentioning

confidence: 99%

Seventy-Five Years of Research on Protein Binding

Dalhoff

2018

Antimicrob Agents Chemother

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This review summarizes evidence that the impact of protein binding of the activity of antibiotics is multifaceted and more complex than indicated by the numerical value of protein binding alone. A plethora of studies has proven that protein binding of antibiotics matters, as the free fraction only is antibacterially active and governs pharmacokinetics. Several studies have indicated that independent from protein binding of immunoglobulin G, albumin, α-acid-glycoprotein, and pulmonary surfactant acted synergistically with antibacterial agents, thus suggesting that some intrinsic properties of serum proteins may have mediated serum-antibiotic synergisms. It has been demonstrated that IgG and albumin permeabilized Gram-negative and Gram-positive bacteria and facilitated the uptake of poorly penetrating antibiotics. Alpha-1-acid-glycoprotein and pulmonary surfactant also exerted a permeabilizing activity, but proof that this property results in a sensitizing effect is missing. The permeabilizing effect of serum proteins may explain why serum-antibiotic synergisms do not represent a general phenomenon but are limited to specific drug-bug associations only. Although evidence has been generated to support the hypothesis that native serum proteins interact synergistically with antibiotics, systematic and well-controlled studies have to be performed to substantiate this phenomenon. The interactions between serum proteins and bacterial surfaces are driven by physicochemical forces. However, preparative techniques, storage conditions, and incubation methods have a significant impact on the intrinsic activities of these serum proteins affecting serum-antibiotic synergisms, so these techniques have to be standardized; otherwise, contradictory data or even artifacts will be generated.

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Section: Albumin and ␣ 1 -Acidic-glycoproteinmentioning

confidence: 99%

Seventy-Five Years of Research on Protein Binding

Dalhoff

2018

Antimicrob Agents Chemother

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“…Previous studies have shown that Man-BSA, prepared by the conjugation of carboxyl groups with p -aminophenyl α- d -mannopyranoside, demonstrates membrane-damaging activity [5]. Therefore, p -aminophenyl α- d -mannopyranoside was used to modify carboxyl groups in OVA.…”

Section: Resultsmentioning

confidence: 99%

“…Amino acid analysis, SDS-PAGE analysis, and HPLC analysis were performed in essentially the same manner as previously described [5,34]. All data are presented as the mean ± SD.…”

Section: Methodsmentioning

confidence: 99%

“…Accordingly, one may imagine that chemical modification potentially causes a change in the membrane-interacting mode of BSA. Although BSA does not demonstrate membrane-perturbing activity, mannosylated bovine serum albumin (Man-BSA) prepared by the conjugation of carboxyl groups with p -aminophenyl α-dextro ( d )-mannopyranoside, exhibits membrane-damaging activity on the lipid-water interface [5]. These results suggest that protein with a membrane-binding capability can show membrane-perturbing activities after the glycation of its carboxyl groups.…”

Section: Introductionmentioning

confidence: 99%

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Ovalbumin with Glycated Carboxyl Groups Shows Membrane-Damaging Activity

Tang

Shi

Chen

et al. 2017

IJMS

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The aim of the present study was to investigate whether glycated ovalbumin (OVA) showed novel activity at the lipid-water interface. Mannosylated OVA (Man-OVA) was prepared by modification of the carboxyl groups with p-aminophenyl α-dextro (d)-mannopyranoside. An increase in the number of modified carboxyl groups increased the membrane-damaging activity of Man-OVA on cell membrane-mimicking vesicles, whereas OVA did not induce membrane permeability in the tested phospholipid vesicles. The glycation of carboxyl groups caused a notable change in the gross conformation of OVA. Moreover, owing to their spatial positions, the Trp residues in Man-OVA were more exposed, unlike those in OVA. Fluorescence quenching studies suggested that the Trp residues in Man-OVA were located on the interface binds with the lipid vesicles, and their microenvironment was abundant in positively charged residues. Although OVA and Man-OVA showed a similar binding affinity for lipid vesicles, the lipid-interacting feature of Man-OVA was distinct from that of OVA. Chemical modification studies revealed that Lys and Arg residues, but not Trp residues, played a crucial role in the membrane-damaging activity of Man-OVA. Taken together, our data suggest that glycation of carboxyl groups causes changes in the structural properties and membrane-interacting features of OVA, generating OVA with membrane-perturbing activities at the lipid-water interface.

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“…In our study, 29 glycation sites of albumin were also detected, only in PEW (Table S1). It was previously suggested that glycated bovine serum albumin has some membrane perturbing activities, enhancing its interaction with membranes and inducing membrane leakage (Yang et al ., 2014). The lysine glycation sites ( n = 29) occurred in albumin were evenly spread over the protein sequence.…”

Section: Discussionmentioning

confidence: 99%

Identification of preserved egg white protein glycation and insight into the bioactivity

Wang

Meng

Qiu

et al. 2022

Int J of Food Sci Tech

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Preserved eggs have been reported to possess anti-inflammatory and antioxidant bioactivities, which are enhanced after protein glycation. However, it is still unknown which proteins are glycated during pickling process of preserved eggs and whether the glycated proteins are related to the bioactivity of preserved eggs. In this study, UPLC-ESI-MS/MS was used to identify glycation of proteins in preserved egg white (PEW) and duck egg white (DEW). Altogether, 142 sites on 53 glycated proteins were detected in PEW while 9 sites on 2 glycated proteins were found in DEW. Bioinformatic analysis suggested that the glycation of PEW proteins (e.g. Ovalbumin, Ovotransferrin, Albumin) were supposed to be connected with allergenicity reduction, and the enhancement of antibacterial and antioxidant bioactivities. These findings provide some indications for the future studies on the detailed bioactivities of glycated proteins in PEW, and pave the way for applied research on glycation and the development of functional foods.

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Bovine serum albumin with glycated carboxyl groups shows membrane-perturbing activities

Cited by 9 publications

References 41 publications

Seventy-Five Years of Research on Protein Binding

Seventy-Five Years of Research on Protein Binding

Ovalbumin with Glycated Carboxyl Groups Shows Membrane-Damaging Activity

Identification of preserved egg white protein glycation and insight into the bioactivity

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