Protein interactions with negatively charged inorganic surfaces

Karina Kubiak-Ossowska, Barbara Jachimska, Mohammed Al Qaraghuli, Paul A. Mulheran

Research output: Contribution to journalReview article

1 Citation (Scopus)

Abstract

Protein adsorption on charged inorganic solid materials has recently attracted enormous interest owing to its various possible applications, including drug delivery and biomaterial design. The need to combine experimental and computational approaches to get a detailed picture of the adsorbed protein properties is increasingly recognised and emphasised in this review. We discuss the methods frequently used to study protein adsorption and the information they can provide. We focus on model systems containing a silica surface, which is negatively charged and hydrophilic at physiological pH, and two contrasting proteins: bovine serum albumin (BSA) and lysozyme (LSZ) that are both water soluble. At pH 7, BSA has a net negative charge, whereas LSZ is positive. In addition, BSA is moderately sized and flexible, whereas LSZ is small and relatively rigid. These differences in charge and structural nature capture the role of electrostatics and hydrophobic interactions on the adsorption of these proteins, along with the impact of adsorption on protein orientation and function. Understanding these model systems will undoubtedly enhance the potential to extrapolate our knowledge to other systems of interest.

LanguageEnglish
Pages104-117
Number of pages14
JournalCurrent Opinion in Colloid and Interface Science
Volume41
Early online date8 Feb 2019
DOIs
Publication statusPublished - 1 Jun 2019

Fingerprint

proteins
Proteins
lysozyme
Muramidase
Bovine Serum Albumin
albumins
serums
Adsorption
adsorption
Enzymes
interactions
Biocompatible Materials
Drug delivery
Biomaterials
Silicon Dioxide
Electrostatics
delivery
drugs
Silica
electrostatics

Keywords

  • bovine serum albumin
  • hydrophobicity
  • lysozyme
  • MD
  • protein adsorption
  • silica

Cite this

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title = "Protein interactions with negatively charged inorganic surfaces",
abstract = "Protein adsorption on charged inorganic solid materials has recently attracted enormous interest owing to its various possible applications, including drug delivery and biomaterial design. The need to combine experimental and computational approaches to get a detailed picture of the adsorbed protein properties is increasingly recognised and emphasised in this review. We discuss the methods frequently used to study protein adsorption and the information they can provide. We focus on model systems containing a silica surface, which is negatively charged and hydrophilic at physiological pH, and two contrasting proteins: bovine serum albumin (BSA) and lysozyme (LSZ) that are both water soluble. At pH 7, BSA has a net negative charge, whereas LSZ is positive. In addition, BSA is moderately sized and flexible, whereas LSZ is small and relatively rigid. These differences in charge and structural nature capture the role of electrostatics and hydrophobic interactions on the adsorption of these proteins, along with the impact of adsorption on protein orientation and function. Understanding these model systems will undoubtedly enhance the potential to extrapolate our knowledge to other systems of interest.",
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Protein interactions with negatively charged inorganic surfaces. / Kubiak-Ossowska, Karina; Jachimska, Barbara; Al Qaraghuli, Mohammed; Mulheran, Paul A.

In: Current Opinion in Colloid and Interface Science , Vol. 41, 01.06.2019, p. 104-117.

Research output: Contribution to journalReview article

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AU - Kubiak-Ossowska, Karina

AU - Jachimska, Barbara

AU - Al Qaraghuli, Mohammed

AU - Mulheran, Paul A.

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AB - Protein adsorption on charged inorganic solid materials has recently attracted enormous interest owing to its various possible applications, including drug delivery and biomaterial design. The need to combine experimental and computational approaches to get a detailed picture of the adsorbed protein properties is increasingly recognised and emphasised in this review. We discuss the methods frequently used to study protein adsorption and the information they can provide. We focus on model systems containing a silica surface, which is negatively charged and hydrophilic at physiological pH, and two contrasting proteins: bovine serum albumin (BSA) and lysozyme (LSZ) that are both water soluble. At pH 7, BSA has a net negative charge, whereas LSZ is positive. In addition, BSA is moderately sized and flexible, whereas LSZ is small and relatively rigid. These differences in charge and structural nature capture the role of electrostatics and hydrophobic interactions on the adsorption of these proteins, along with the impact of adsorption on protein orientation and function. Understanding these model systems will undoubtedly enhance the potential to extrapolate our knowledge to other systems of interest.

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