Infrared Study of the Effect of Hydration on the Amide I Band and Aggregation Properties of Helical Peptides

Mukherjee, Smita; Chowdhury, P. K.; Gai, Feng

doi:10.1021/jp0689060

Cited by 81 publications

(123 citation statements)

References 62 publications

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“…S4) indicating that the association observed by AUC corresponded to the formation of helical bundles. The IR spectra in the amide I region of the FPs shows a single, sharp peak at 1656 cm −1 , indicative of a dehydrated helical conformation (66) in bilayers ( Fig. 2 A and B).…”

Section: Resultsmentioning

confidence: 99%

Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion

Donald¹,

Zhang

Fiorin

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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Membrane fusion is required for diverse biological functions ranging from viral infection to neurotransmitter release. Fusogenic proteins increase the intrinsically slow rate of fusion by coupling energetically downhill conformational changes of the protein to kinetically unfavorable fusion of the membrane-phospholipid bilayers. Class I viral fusogenic proteins have an N-terminal hydrophobic fusion peptide (FP) domain, important for interaction with the target membrane, plus a C-terminal transmembrane (C-term-TM) helical membrane anchor. The role of the water-soluble regions of fusogenic proteins has been extensively studied, but the contributions of the membrane-interacting FP and C-term-TM peptides are less well characterized. Typically, FPs are thought to bind to membranes at an angle that allows helix penetration but not traversal of the lipid bilayer. Here, we show that the FP from the paramyxovirus parainfluenza virus 5 fusogenic protein, F, forms an N-terminal TM helix, which self-associates into a hexameric bundle. This FP also interacts strongly with the C-term-TM helix. Thus, the fusogenic F protein resembles SNARE proteins involved in vesicle fusion by having water-soluble coiled coils that zipper during fusion and TM helices in both membranes. By analogy to mechanosensitive channels, the force associated with zippering of the water-soluble coiled-coil domain is expected to lead to tilting of the FP helices, promoting interaction with the C-term-TM helices. The energetically unfavorable dehydration of lipid headgroups of opposing bilayers is compensated by thermodynamically favorable interactions between the FP and C-term-TM helices as the coiled coils zipper into the membrane phase, leading to a pore lined by both lipid and protein.T he basic mechanisms of viral membrane fusion have been studied extensively, but major gaps remain in our understanding of the relative roles of lipidic intermediates and viral fusogenic proteins in lowering the energy barrier for the overall process (1-4). The most common mechanistic hypothesis concerning enveloped viral fusion is that fusogenic proteins primarily serve to bring the target cell and viral membranes into proximity. Fusion occurs in a multistep process, in which the virus first binds to a specific receptor; this event and/or other environmental cues then cause a conformational change in the protein, leading to a metastable state with an exposed hydrophobic fusion peptide (FP) that binds to the target membrane. Once engaged with the bilayer, a second energetically favorable conformational change in the fusogenic protein then exerts a force pulling the FP toward the viral membrane, in effect reeling the host and viral membranes together.The conformational changes involved in the water-soluble portions of viral fusogenic proteins have been largely elucidated, but the roles of the membrane-binding FP and the C-terminal transmembrane (C-term-TM) anchor are less clear. After the crystal structure of the prefusogenic form of influenza hemagglutinin (HA) was solved...

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Section: Resultsmentioning

confidence: 99%

Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion

Donald¹,

Zhang

Fiorin

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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“…6K-F17) largely retains its ␣-helical conformation upon entering the membrane. This phenomenon is likely attributable to a charge neutralization effect as the peptides bind to the surface of the anionic bacterial membranes, and the resulting dehydrated environment facilitates the formation of ␤-strand-type aggregates of the CAP with a sequence of higher hydrophobicity (34,35). This result indicates that (overly) high core segmental hydrophobicity can lead to an increased potential to peptide self-association at the membrane surface (and possibly to precipitation), thus limiting the concentration of peptide actually impacting on the bacterial membrane and consequently reducing antimicrobial activity; this latter notion is supported by the relatively lower MIC for the 6K-F17 peptide (4 M) versus its Leu-containing counterpart (16 M).…”

Section: Discussionmentioning

confidence: 99%

Roles of Hydrophobicity and Charge Distribution of Cationic Antimicrobial Peptides in Peptide-Membrane Interactions

Yin

Edwards

et al. 2012

Journal of Biological Chemistry

339

230

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Background: Cationic antimicrobial peptides offer an alternative to conventional antibiotics, as they physically disrupt bacterial membranes, causing cell death. Results: Peptides designed with high hydrophobicity display strong self-association that is minimized by distribution of positive charges at both peptide termini. Conclusion: Balancing peptide hydrophobicity and charge distribution promotes efficient antimicrobial activity. Significance: Routes to optimization of peptide sequences are valuable for devising therapeutic strategies.

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“…Thus, excessive addition of the MTGase did not affect the OH stretching vibration of protein. The changes of water structure also affected the secondary structure of meat protein, the stronger hydrogen bonding promotes secondary structural transitions toward β-sheets (Mukherjee, Chowdhury, & Gai, 2007).…”

Section: Water Structurementioning

confidence: 99%

Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

Kang

2016

CyTA - Journal of Food

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Microbial transglutaminase (MTGase) is a kind of enzyme preparation which is used in the processing of emulsified meat products for improving the quality. In this paper, the effect of MTGase content on water-holding capacity, texture and protein structure was studied by using Raman spectroscopy. The results showed that emulsion stability and cooking yield were significantly (P < 0.05) improved with increased MTGase content. But when the contents were 0.67% and 1%, the emulsion stability and cooking yield had no significant difference (P > 0.05). The hardness, springiness, cohesiveness and chewiness also were significantly (P < 0.05) improved with increased MTGase content. The result of Raman spectroscopy found that the wave peak of amide I shifted from 1658 to 1660, 1661 and 1661 cm −1 when added various amounts of MTGase, β-sheet and β-turn contents were significantly (P < 0.05) increased with decreased α-helix content, and random coil was not a significant difference (P > 0.05); the wave peak of 3100-3500 cm −1 shifted from 3226 to 3228, 3229 and 3229 cm −1 that indicated OH stretching motions were stronger. Overall, when added appropriately, MTGase to frankfurters could change the protein conformation, improve the texture and water-holding capacity.Efecto de los niveles de transglutaminasa en las salchichas Frankfurt: Un estudio fisicoquímico y espectroscopia Raman RESUMEN La transglutaminasa microbial (MTGase) es un tipo de preparado encimático utilizado en el procesamiento de productos cárnicos emulsionados para mejorar su calidad. En este estudio se ha investigado el efecto del contenido de MTGase en la capacidad de retención de agua, la textura y la estructura proteínica mediante la utilización de espectroscopia Raman. Los resultados mostraron que la estabilidad de emulsión y el rendimiento de cocinado mejoraron significativamente (P < 0,05) con el aumento del contenido de MTGase. Sin embargo, cuando los contenidos fueron 0,67% y 1%, la estabilidad de emulsión y el rendimiento de cocinado no obtuvieron diferencias significativas (P > 0,05). La dureza, la ligereza, la cohesión y la masticabilidad también fueron mejorados significativamente (P < 0,05) con el aumentó en el contenido de MTGase. Los resultados de la espectroscopia Raman indicaron que la ola pico de amida I cambió de 1658 cm −1 a 1660 cm, 1661 cm −y y 1661 cm −1 cuando fueron añadidas diferentes cantidades de Migase. Los contenidos de lámina β y giro β aumentaron significativamente (P < 0,05) cuando el contenido de hélice α disminuyó, además el movimiento aleatorio no fue significativamente diferente (P > 0,05); la ola pico de 3100-3500 cm , lo cual indicó que los movimientos de elasticidad de OH eran más fuertes. En general, la adición apropiada de MTGase a las salchichas Frankfurt podría cambiar la conformación proteínica, mejorar la textura y la capacidad de retención de agua. ARTICLE HISTORY

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Infrared Study of the Effect of Hydration on the Amide I Band and Aggregation Properties of Helical Peptides

Cited by 81 publications

References 62 publications

Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion

Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusion

Roles of Hydrophobicity and Charge Distribution of Cationic Antimicrobial Peptides in Peptide-Membrane Interactions

Effect of the levels of transglutaminase in frankfurters: a physical–chemical and Raman spectroscopy study

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