Role of hydrophobic and hydrophilic forces in peptide-protein interaction: New advances

Cserháti, Tibor; Szőgyi, M.

doi:10.1016/0196-9781(94)00134-r

Cited by 30 publications

(24 citation statements)

References 100 publications

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“…A possible explanation for this observation is that the antibodybinding site might be masked by conformational changes that are induced as a result of the adsorption of the amylase molecule to the pellicle surface (19). Owing to the embedding procedure of the ultrathin section, some protein epitopes may be hidden, thus hindering specific binding of the antibody.…”

Section: Discussionmentioning

confidence: 99%

Electron microscopic detection of salivary α‐amylase in the pellicle formed in situ

Deimling

Breschi

Hoth-Hannig

et al. 2004

European J Oral Sciences

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Immunological and biochemical analyses have shown that alpha-amylase is an essential component of the acquired pellicle. After adsorption, this enzyme might act as a receptor for bacterial adherence. However, data indicating that amylase is bound to the pellicle surface in vivo and thus available for adhering bacteria are rare. Therefore, the present study focused on alpha-amylase within the pellicle formed in situ, using gold-immunolabeling electron microscopic techniques. Pellicles were formed by intra-oral exposure of enamel specimens for 30 and 120 min in six subjects. The results obtained by transmission electron microscopy indicate that amylase was randomly distributed in the pellicle layer without any preferential localization within the pellicle. Thus, salivary alpha-amylase might be considered as an important structural component that is even involved in the early stages of pellicle formation. The findings of field emission in-lens scanning electron microscopy provided evidence that the enzyme is located on the pellicle surface. It could be concluded that alpha-amylase might act as a receptor for bacterial adherence to the pellicle in vivo.

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Section: Discussionmentioning

confidence: 99%

Electron microscopic detection of salivary α‐amylase in the pellicle formed in situ

Deimling

Breschi

Hoth-Hannig

et al. 2004

European J Oral Sciences

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“…The importance of hydrophobic forces in peptide-protein interactions have been reviewed [50], and the principles can be extended to the amino acid residues wrapping the NPs synthesized here and proteins present in the outer bacterial wall and membrane. Our findings give new and relevant insights when the synthesis of effective nanoparticulate systems, designed to capture microbial cells, is the goal.…”

Section: Discussionmentioning

confidence: 99%

Hydrophobic Forces Are Relevant to Bacteria-Nanoparticle Interactions: Pseudomonas putida Capture Efficiency by Using Arginine, Cysteine or Oxalate Wrapped Magnetic Nanoparticles

Figueredo

Saavedra

Cortón

et al. 2018

Colloids and Interfaces

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Size, shape and surface characteristics strongly affect interfacial interactions, as the presented among iron oxide nanoparticles (NPs) aqueous colloids and bacteria. In other to find the forces among this interaction, we compare three types of surface modified NPs (exposing oxalate, arginine or cysteine residues), based on a simple synthesis and derivation procedure, that allows us to obtain very similar NPs (size and shape of the magnetic core). In this way, we assure that the main difference in the synthesized NPs are the oxalate or amino acid residue exposed, an ideal situation to compare their bacterial capture performance, and so too the interactions among them. Field emission scanning electron microscopy showed homogeneous distribution of particle sizes for all systems synthesized, close to 10 nm. Magnetization, zeta potential, Fourier transformed infrared spectrometry and other studies allow us further characterization. Capture experiments of Pseudomonas putida bacterial strain showed a high level of efficiency, independently of the amino acid used to wrap the NP, when compared with oxalate. We show that bacterial capture efficiency cannot be related mostly to the bacterial and NP superficial charge relationship (as determined by z potential), but instead capture can be correlated with hydrophobic and hydrophilic forces among them.

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“…As the polypeptide chain grows even more, the protein will fold spontaneously to the most thermodynamically stable, tertiary structure by confining the most hydrophobic regions to the interior to minimize the interaction with water. 3 The capacity of a RPC column to purify a peptide is related to the amount of surface area that can bind to the nonpolar stationary phase, as mentioned previously. Because a large polypeptide or protein has more surface area, a RP C-18 column is not as efficient in separating.…”

Section: Hydrophilicity and Hydrophobicitymentioning

confidence: 99%

Biomolecules

Olszowy¹,

Burns²,

Ciborowski³

2013

Proteomic Profiling and Analytical Chemistry

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Role of hydrophobic and hydrophilic forces in peptide-protein interaction: New advances

Cited by 30 publications

References 100 publications

Electron microscopic detection of salivary α‐amylase in the pellicle formed in situ

Electron microscopic detection of salivary α‐amylase in the pellicle formed in situ

Hydrophobic Forces Are Relevant to Bacteria-Nanoparticle Interactions: Pseudomonas putida Capture Efficiency by Using Arginine, Cysteine or Oxalate Wrapped Magnetic Nanoparticles

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