Peptoid Residues Make Diverse, Hyperstable Collagen Triple-Helices

2021 ◽  
Author(s):  
Julian L. Kessler ◽  
Grace Kang ◽  
Zhao Qin ◽  
Helen Kang ◽  
Frank G. Whitby ◽  
...  
Keyword(s):  
Triple Helices

DNA triple helices. A molecular dynamics study

1991 ◽  
Vol 88 ◽  
pp. 2597-2603 ◽  
Author(s):  
CA Laughton ◽  
S Neidle
Keyword(s):  
Molecular Dynamics ◽  
Triple Helices

scholarly journals Thermally-Induced Shape-Memory Behavior of Degradable Gelatin-Based Networks

2021 ◽  
Vol 22 (11) ◽  
pp. 5892
Author(s):  
Axel T. Neffe ◽  
Candy Löwenberg ◽  
Konstanze K. Julich-Gruner ◽  
Marc Behl ◽  
Andreas Lendlein
Keyword(s):  
Shape Memory ◽  
Shape Memory Effect ◽  
Memory Effect ◽  
Shape Recovery ◽  
Polymer Networks ◽  
Water Soluble ◽  
Compression Tests ◽  
Thermally Induced ◽  
Thermomechanical Process ◽  
Triple Helices

Shape-memory hydrogels (SMH) are multifunctional, actively-moving polymers of interest in biomedicine. In loosely crosslinked polymer networks, gelatin chains may form triple helices, which can act as temporary net points in SMH, depending on the presence of salts. Here, we show programming and initiation of the shape-memory effect of such networks based on a thermomechanical process compatible with the physiological environment. The SMH were synthesized by reaction of glycidylmethacrylated gelatin with oligo(ethylene glycol) (OEG) α,ω-dithiols of varying crosslinker length and amount. Triple helicalization of gelatin chains is shown directly by wide-angle X-ray scattering and indirectly via the mechanical behavior at different temperatures. The ability to form triple helices increased with the molar mass of the crosslinker. Hydrogels had storage moduli of 0.27–23 kPa and Young’s moduli of 215–360 kPa at 4 °C. The hydrogels were hydrolytically degradable, with full degradation to water-soluble products within one week at 37 °C and pH = 7.4. A thermally-induced shape-memory effect is demonstrated in bending as well as in compression tests, in which shape recovery with excellent shape-recovery rates Rr close to 100% were observed. In the future, the material presented here could be applied, e.g., as self-anchoring devices mechanically resembling the extracellular matrix.

End-stapled homo and hetero collagen triple helices: a click chemistry approach

2011 ◽  
Vol 47 (9) ◽  
pp. 2589-2591 ◽  
Author(s):  
Cillian Byrne ◽  
Paul A. McEwan ◽  
Jonas Emsley ◽  
Peter M. Fischer ◽  
Weng C. Chan
Keyword(s):  
Click Chemistry ◽  
Triple Helices

scholarly journals Application of Cu(I)-catalyzed azide–alkyne cycloaddition for the design and synthesis of sequence specific probes targeting double-stranded DNA

2016 ◽  
Vol 12 ◽  
pp. 1348-1360 ◽  
Author(s):  
Svetlana V Vasilyeva ◽  
Vyacheslav V Filichev ◽  
Alexandre S Boutorine
Keyword(s):  
Minor Groove ◽  
Binding Parameters ◽  
Design And Synthesis ◽  
Minor Groove Binders ◽  
Double Stranded Dna ◽  
Triple Helices ◽  
Gel Shift ◽  
Groove Binders

Efficient protocols based on Cu(I)-catalyzed azide–alkyne cycloaddition were developed for the synthesis of conjugates of pyrrole–imidazole polyamide minor groove binders (MGB) with fluorophores and with triplex-forming oligonucleotides (TFOs). Diverse bifunctional linkers were synthesized and used for the insertion of terminal azides or alkynes into TFOs and MGBs. The formation of stable triple helices by TFO-MGB conjugates was evaluated by gel-shift experiments. The presence of MGB in these conjugates did not affect the binding parameters (affinity and triplex stability) of the parent TFOs.

scholarly journals Hybrid gelation processes in enzymatically gelled gelatin: impact on nanostructure, macroscopic properties and cellular response

Soft Matter ◽  
2013 ◽  
Vol 9 (29) ◽  
pp. 6986-6999 ◽  
Author(s):  
Franziska Bode ◽  
Marcelo Alves da Silva ◽  
Paul Smith ◽  
Christian D. Lorenz ◽  
Seth McCullen ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Cellular Response ◽  
Cross Linking ◽  
Cluster Growth ◽  
Macroscopic Properties ◽  
Physical Gelation ◽  
Triple Helices

Enzymatic cross-linking of gelatin (left) proceeds through cluster growth (red); when combined with physical gelation, clusters are constrained by triple-helices (black), yielding a more ordered and efficient network, favouring cell proliferation.

Recognition of CG inversions in DNA triple helices by methylated 3H-pyrrolo[2,3-d]pyrimidin-2(7H)-one nucleoside analogues

2005 ◽  
pp. 2555 ◽  
Author(s):  
Rohan T. Ranasinghe ◽  
David A. Rusling ◽  
Vicki E. C. Powers ◽  
Keith R. Fox ◽  
Tom Brown
Keyword(s):  
Nucleoside Analogues ◽  
Triple Helices

scholarly journals Structural diversity and domain composition of a unique collagenous fragment (intima collagen) obtained from human placenta

1983 ◽  
Vol 211 (2) ◽  
pp. 295-302 ◽  
Author(s):  
E Odermatt ◽  
J Risteli ◽  
V van Delden ◽  
R Timpl
Keyword(s):  
Human Placenta ◽  
Triple Helix ◽  
Structural Diversity ◽  
Helical Conformation ◽  
Basic Unit ◽  
Bacterial Collagenase ◽  
Disulphide Bonds ◽  
Triple Helices ◽  
Electron Microscopical ◽  
Polypeptide Chains

Intima collagen was obtained from pepsin digests of human placenta in two forms, which differ to some extent in the size of their constituent polypeptide chains (Mr 50 000-70 000). These chains are connected by disulphide bonds to large aggregates. The aggregates are arranged in a triple-helical conformation with a remarkably high thermal stability (Tm 41-62 degrees C) and are resistant to further proteolytic digestion. Reduction of as little as 5% of the disulphide bonds produces mainly monomeric triple helices (Mr about 160 000) with Tm 32 degrees C. Partially reduced material can be separated into triple-helical and non-collagenous domains by proteolysis. Pepsin releases a collagenous component with chains of Mr 38 000. Bacterial collagenase liberates two non-collagenous segments (Mr 15 000-30 000) rich in cystine. Treatment with collagenase before reduction separates intima collagen into a large fragment composed of collagenous (Tm 41 degrees C) and non-collagenous structures and a single non-collagenous segment. The data support the electron-microscopical model of intima collagen [Furthmayr, Wiedemann, Timpl, Odermatt & Engel (1983) Biochem. J. 211, 303-311], indicating that the basic unit of the fragment consists of a continuous triple helix joining two globular domains.

RNA and Triple Helices

1999 ◽  
pp. 233-242 ◽  
Author(s):  
Kyonggeun Yoon ◽  
Jörg Jendis ◽  
Karin Moelling
Keyword(s):  
Triple Helices
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