Characterization of the Interaction Between Pancreatic Trypsin and an Enteric Copolymer as a Tool for Several Biotechnological Applications

Braia, Mauricio; Loureiro, Dana Belén; Tubío, Gisela; Romanini, Diana

doi:10.1016/j.colsurfb.2015.10.037

Cited by 5 publications

(4 citation statements)

References 23 publications

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“…44 (Notably, this protein was slightly destabilized by the 1:2 (i.e., more hydrophobic) co-polymer. 56 ) Finally, the secondary structure of bovine serum albumin has been shown to be stabilized�at pH extremes, high urea concentration, and high temperature� when confined within a polyelectrolyte complex coacervate phase. 48 As stated above, there are also many reports of protein destabilization upon polyelectrolyte assembly, and an important common theme appears to be polymer hydrophobicity.…”

Section: ■ Discussionmentioning

confidence: 99%

“…Trypsin has been reported to be stabilized through interaction with Eudragit L100, a 1:1 co-polymer of methacrylic acid and (hydrophobic) methyl methacrylic acid . (Notably, this protein was slightly destabilized by the 1:2 (i.e., more hydrophobic) co-polymer …”

Section: Discussionmentioning

confidence: 99%

“…Over a broad range of applications and morphologies, an important overarching question is how the polymer component influences the structure and function of the protein. Stabilization is often desired, and in many instances, proteins interacting with charged polymers are indeed stabilized against thermal or chemical stresses. − However, other studies show little effect or even a destabilizing influence. − Despite its clear importance to many technologies, our current understanding of the influence of polyelectrolyte assembly on protein structure and function is quite limited.…”

Section: Introductionmentioning

confidence: 99%

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Polyelectrolyte Influence on Beta-Hairpin Peptide Stability: A Simulation Study

Moses

Tassel

2022

J. Phys. Chem. B

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Assemblies of proteins and charged macromolecules (polyelectrolytes) find important applications as pharmaceutical formulations, biocatalysts, and cell-contacting substrates. A key question is how the polymer component influences the structure and function of the protein. The present paper addresses the influence of charged polymers on the thermal stability of two model beta-hairpin-forming peptides through an all-atom, replica exchange molecular dynamics simulation. The (negatively charged) peptides consist of the terminal 16 amino acids of the B1 domain of Protein G (GB1) and a variant with three of the GB1 residues substituted with tryptophan (Tryptophan Zipper 4, or TZ4). A (cationic) lysine polymer is seen to thermally stabilize TZ4 and destabilize GB1, while a (also cationic) chitosan polymer slightly stabilizes GB1 but has essentially no effect on TZ4. Free energy profiles reveal folded and unfolded conformations to be separated by kinetic barriers generally acting in the direction of the thermodynamically favored state. Through application of an Ising-like statistical mechanical model, a mechanism is proposed based on competition between (indirect) entropic stabilization of folded versus unfolded states and (direct) competition for hydrogen-bonding and hydrophobic interactions. These findings have important implications to the design of polyelectrolyte-based materials for biomedical and biotechnological applications.

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Section: ■ Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Polyelectrolyte Influence on Beta-Hairpin Peptide Stability: A Simulation Study

Moses

Tassel

2022

J. Phys. Chem. B

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“…The precipitation of these complexes depends on different experimental parameters such as concentration, number and distribution of charged sites on the components, protein-polyelectrolyte ratio, pH and ionic strength of the medium, etc. [8][9][10].…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%