Influence of central sidechain on self-assembly of glycine-x-glycine peptides

Thursch, Lavenia; Lima, Thamires A.; O'Neill, Nichole; Ferreira, Fábio Furlan; Schweitzer‐Stenner, Reinhard; Alvarez, Nicolas J.

doi:10.1039/d2sm01082h

Cited by 8 publications

(4 citation statements)

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“…The calculated solubility and softening temperature for GHG are higher compared to other investigated GXG peptides 14 . Stabilization of the GHG fibrils outlined in this paper could be due to the hydrogen bonding capacity of the imidazole which can function as both a donor and acceptor.…”

Section: Discussionmentioning

confidence: 67%

“…The work described in this paper focused on exploring the thermal stability of GHG gels in the absence and presence of chaotropic (Mg 2+ , NO 3 − ) and kosmotropic ions (NH 4 + , H 2 PO 4 − , CH 3 COO − ). Recent rheological experiments indicated that the GHG gel is significantly more thermally stable than the gel phase of other GxG peptides (GAG in water/ethanol, GWG, GYG and GFG in water) 14 . We quantitatively assess the thermal stability of GHG gels by using rheology and UVCD spectroscopy.…”

Section: Introductionmentioning

confidence: 99%

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Tuning the thermostability of GHG gels by salts at different positions on the Hofmeister scale

O’Neill,

Alvarez,

Schweitzer-Stenner

2024

Sci Rep

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The influence of Hofmeister cations (NH4+, Na+, Mg2+) and anions (H2PO4−, CH3COO−, Cl−, NO3−) on the thermostability of a GHG hydrogel was investigated. The combined results of UV circular dichroism (UVCD) and Small Amplitude Oscillatory Shear Rheology experiments reveal that the addition of salt reduces the stability of the gel phase and the underlying fibrils. In line with the cationic Hofmeister hierarchy, the chaotropic Mg2+ ions caused the greatest thermal destabilization of the gel phase with the gel → sol transition temperature Tgs value lowered by 10 °C. In the absence of salt, the gel → sol transition probed by the storage modulus and microscopy is biphasic. In the presence of salt, it becomes monophasic. Contrary to expectations the presence of Hofmeister anions leads to a nearly identical reduction of the gel → sol transition temperatures. However, UVCD spectra suggest that they affect the ππ-stacking between imidazole groups to a different extent. We relate the absence of ion specificity regarding the solubility of fibrils (probed by UVCD) to the observed enthalpy-entropy compensation of the dissolution process. Our results combined show how CD spectroscopy and rheology combined yields a more nuanced picture of the processes underlying the gel → sol transition.

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Section: Discussionmentioning

confidence: 67%

Section: Introductionmentioning

confidence: 99%

Tuning the thermostability of GHG gels by salts at different positions on the Hofmeister scale

O’Neill,

Alvarez,

Schweitzer-Stenner

2024

Sci Rep

Self Cite

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“…They also exhibit mucus‐like shear‐thinning behavior 62 and hysteresis in steady shear experiments, indicative of a self‐assembled superstructure. When comparing the hFF03 hydrogels to other reported peptide hydrogels, G 0 at 0.5% (w/v) as a measure of gel strength is two orders of magnitude smaller than for the Fmoc‐FF motif 63 and almost four orders of magnitude smaller than for some of the GxG series 64 . The MAX series (MAX8 peptide 65 ) exhibits a G 0 that is 3‐fold larger than that of hFF03‐based gels.…”

Section: Resultsmentioning

confidence: 84%

Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels

Proksch,

Dal Colle,

Heinz

et al. 2024

Journal of Peptide Science

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Mucus is a complex biological hydrogel that acts as a barrier for almost everything entering or exiting the body. It is therefore of emerging interest for biomedical and pharmaceutical applications. Besides water, the most abundant components are the large and densely glycosylated mucins, glycoproteins of up to 20 MDa and carbohydrate content of up to 80 wt%. Here, we designed and explored a library of glycosylated peptides to deconstruct the complexity of mucus. Using the well‐characterized hFF03 coiled‐coil system as a hydrogel‐forming peptide scaffold, we systematically probed the contribution of single glycans to the secondary structure as well as the formation and viscoelastic properties of the resulting hydrogels. We show that glycan‐decoration does not affect α‐helix and coiled‐coil formation while it alters gel stiffness. By using oscillatory macrorheology, dynamic light scattering microrheology, and fluorescence lifetime‐based nanorheology, we characterized the glycopeptide materials over several length scales. Molecular simulations revealed that the glycosylated linker may extend into the solvent, but more frequently interacts with the peptide, thereby likely modifying the stability of the self‐assembled fibers. This systematic study highlights the interplay between glycan structure and hydrogel properties and may guide the development of synthetic mucus mimetics.

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“…Molecular self-assembly is the spontaneous process of forming various ordered structures under thermodynamic and kinetic conditions. [1][2][3][4][5] In recent decades, great efforts have been focused on self-assembled peptide nanostructures owing to their structural simplicity, biocompatibility, chemical versatility, facile synthesis, and widespread applications. [6][7][8][9][10] The ordered organization of peptide molecules into defined nanostructures relies on specific molecular recognition which is facilitated by a combination of non-covalent interactions, including hydrogen bonds, non-specific van der Waals forces, electrostatic interactions, p-p stacking, hydrophobic forces, and chiral dipole-dipole interactions.…”

Section: Introductionmentioning

confidence: 99%

Influence of pH on the self-assembly of diphenylalanine peptides: molecular insights from coarse-grained simulations

Wang

Zhao

et al. 2023

Soft Matter

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Influence of central sidechain on self-assembly of glycine-x-glycine peptides

Abstract: Low molecular weight gelators (LMWG) are the subject of intense research for a range of biomedical, and engineering applications. Peptides are a special class of LMWG, which offer infinite sequence...

Cited by 8 publications

References 80 publications

Tuning the thermostability of GHG gels by salts at different positions on the Hofmeister scale

Tuning the thermostability of GHG gels by salts at different positions on the Hofmeister scale

Impact of glycan nature on structure and viscoelastic properties of glycopeptide hydrogels

Influence of pH on the self-assembly of diphenylalanine peptides: molecular insights from coarse-grained simulations

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