2022
DOI: 10.1039/d1sc06562a
|View full text |Cite
|
Sign up to set email alerts
|

Direct observation of peptide hydrogel self-assembly

Abstract: To facilitate the characterization of phase-transitioning molecules, site-specific non-perturbative infrared probes are leveraged for continuous observation of the self-assembly of fibrils in a peptide hydrogel following stopped-flow initiation.

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1

Citation Types

0
9
0

Year Published

2023
2023
2024
2024

Publication Types

Select...
5

Relationship

0
5

Authors

Journals

citations
Cited by 7 publications
(9 citation statements)
references
References 66 publications
0
9
0
Order By: Relevance
“…Techniques that study infrared absorption, circular dichroism, or fluorescence spectra are able to capture time‐resolved structural changes of biomolecules [45,46] . In addition to quantifying the concentration of a given analyte, spectroscopic methods report on changes in the molecular conformation, [46] environment, [30] and bonding [47] of the analyte. Optical spectroscopy methods may also be enhanced by coupling them with other tools such as pump‐probe, [23] stopped‐flow, [47] or confocal microscopy [30] …”
Section: Approaches To In Situ Characterization Of Biomolecular Assemblymentioning
confidence: 99%
See 3 more Smart Citations
“…Techniques that study infrared absorption, circular dichroism, or fluorescence spectra are able to capture time‐resolved structural changes of biomolecules [45,46] . In addition to quantifying the concentration of a given analyte, spectroscopic methods report on changes in the molecular conformation, [46] environment, [30] and bonding [47] of the analyte. Optical spectroscopy methods may also be enhanced by coupling them with other tools such as pump‐probe, [23] stopped‐flow, [47] or confocal microscopy [30] …”
Section: Approaches To In Situ Characterization Of Biomolecular Assemblymentioning
confidence: 99%
“…In the case of proteins, CD spectra can be fit to extract the proportion of structural motifs, such as β-sheets and α-helices, present in the sample. Time-resolved CD has been used to study the self-assembly of protein structures such as amyloid fibrils, [46] chiral supramolecular structures and hydrogels, [47,[63][64][65] and protein-surfactant complexes. [66] A typical CD spectrum requires several minutes to acquire.…”
Section: Circular Dichroism Spectroscopymentioning
confidence: 99%
See 2 more Smart Citations
“…[64][65][66][67] Various nanostructures of self-assembled peptide materials, such as hydrogels, [68][69][70][71] lipid-like vesicles, 72 and nanofibers, [73][74][75] are ideal candidates for being developed into drug carriers due to their superb packaging ability, safety protection, and precise drug release. Compared to other traditional nano-drug systems, the main advantage of peptide scaffold-based smart nano-drug systems is that they can respond to multi-layered stimuli in vivo, such as microenvironmental stimuli, cellular stimuli (e.g., pH, 76 ionic strength, [77][78][79] receptor-ligand interactions, [80][81][82] specific proteins, 83 or enzymes 84,85 ), and external environmental stimuli (e.g., light, 86 temperature, 87 ultrasound, 88 electric, 89 or magnetic fields 90 ), and can mediate controlled drug release in situ. This mechanism with a dynamic response similar to a carefully designed "autonomous cruise missile" maximizes the killing of tumor targets while avoiding damage to non-target organs, increasing loaded drug bioavailability.…”
mentioning
confidence: 99%