Promotion of the collagen triple helix in a hydrophobic environment

Kubyshkin, Vladimir; Budiša, Nediljko

doi:10.1039/c9ob00070d

Cited by 7 publications

(6 citation statements)

References 35 publications

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“…12b After reporting a hydrophobic P II helix, our recent study on collagen mimicking peptides suggests a possibility for oligomeric P II assemblies in hydrophobic media. 70 Therefore, our discovery of the TM P II helix opens up an avenue for engineering entirely new types of de novo membrane-associated peptide structures, not present in nature but deliberately constructed under laboratory conditions.…”

Section: Discussionmentioning

confidence: 99%

Bilayer thickness determines the alignment of model polyproline helices in lipid membranes

Kubyshkin

Grage

Ulrich

et al. 2019

Phys. Chem. Chem. Phys.

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Section: Discussionmentioning

confidence: 99%

Bilayer thickness determines the alignment of model polyproline helices in lipid membranes

Kubyshkin

Grage

Ulrich

et al. 2019

Phys. Chem. Chem. Phys.

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“…Modification of charged side chains with nonpolar moieties through esterification has been shown to increase cell permeability 21 . While N-acetylated polyproline has been shown to be somewhat soluble in octanol, modification of proline to an indole can also increase hydrophobicity of peptides by further burying the polar backbone and still allows helical conformation 22 , and that structural architectures like collagen can form in octanol with similar modification 23 demonstrating the ability of peptide derivatives to form both secondary and quaternary structures in nonpolar solvents. These findings suggest that biopolymer derivatives would likely be more successful than their water-evolved counterparts.…”

Section: Discussionmentioning

confidence: 99%

Partitioning of amino acids and proteins into decanol using phase transfer agents towards understanding life in non-polar liquids

Thompson

Burt

Lee

et al. 2019

Sci Rep

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Water has many roles in the context of life on Earth, however throughout the universe, other liquids may be able to support the emergence of life. We looked at the ability of amino acids, peptides, a depsipeptide, and proteins to partition into a non-polar decanol phase, with and without the addition of a phase transfer agent. Partitioning evaluated using UV detection, or with HPLC coupled to either charged aerosol detection or ESI-MS. For amino acids and short peptides, phase transfer agents were used to move the biomolecules to the decanol phase, and this transfer was pH dependent. For larger molecules, phase transfer agents did not seem to affect the transfer. Both the depsipetide, valinomycin, and the protein Taq DNA polymerase had solubility in the decanol phase. Additionally, valinomycin appeared to retain its biological ability to bind to potassium ions. These results show that most terrestrial biological molecules are not compatible with non-polar solvents, but it is possible to find and perhaps evolve polymers that are functional in such phases.

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“…Recent studies used this destabilizing effect of co‐solvents or additives on the triple helix to develop a solvent‐switching protocol for targeting damaged collagen in histological samples with collagen hybridizing peptides [25] . Other solvents than water, for example, propane‐1,2‐diol and octan‐1‐ol stabilize CMP trimers to a significant extent [26–27] . Our group showed that a local hydrophobic environment created by lipidation stabilizes collagen triple helices in water [13,28] .…”

Section: Introductionmentioning

confidence: 93%

Carbohydrate Co‐Solutes Stabilize Collagen Triple Helices

Nomura,

Fiala,

Wennemers

2024

ChemBioChem

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Carbohydrates are common co‐solutes for the stabilization of proteins. The effect of carbohydrate solutions on the stability of collagen, the most abundant protein in mammals, is, however, underexplored. In this work, we studied the thermal stability of collagen triple helices derived from a molecularly defined collagen model peptide (CMP), Ac‐(Pro‐Hyp‐Gly)7‐NH2, in solutions of six common mono‐ and disaccharides. We show that the carbohydrates stabilize the collagen triple helix in a concentration‐dependent manner, with an increase of the melting temperature of up to 17 °C. In addition, we show that the stabilizing effect is similar for all studied sugars, including trehalose, which is otherwise considered a privileged bioprotectant. The results provided insight into the effects of sugar co‐solutes on collagen triple helices and can aid the selection of storage environments for collagen‐based materials and probes.

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Promotion of the collagen triple helix in a hydrophobic environment

Abstract: The collagen triple helix is better suited for octanol than for water.

Cited by 7 publications

References 35 publications

Bilayer thickness determines the alignment of model polyproline helices in lipid membranes

Bilayer thickness determines the alignment of model polyproline helices in lipid membranes

Partitioning of amino acids and proteins into decanol using phase transfer agents towards understanding life in non-polar liquids

Carbohydrate Co‐Solutes Stabilize Collagen Triple Helices

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