The crown ether size and stereochemistry affect the self-assembly, hydrogelation, and cellular interactions of crown ether/peptide conjugates

2020 ◽  
Vol 8 (43) ◽  
pp. 9961-9970
Author(s):  
Abdelreheem Abdelfatah Saddik ◽  
Mohiuddin Mohammed ◽  
Hsin-Chieh Lin

Crown ether ring size affects nanofiber morphology of hydrogels upon conjugation with D- and L-phenylalanine dipeptides. Random nanofibers showed enhanced cell adhesion and proliferation whereas twisted nanofibers displayed weak cell attachments.

2007 ◽  
Vol 17 (25) ◽  
pp. 2654 ◽  
Author(s):  
Pim G. A. Janssen ◽  
Pascal Jonkheijm ◽  
Pall Thordarson ◽  
Jeroen C. Gielen ◽  
Peter C. M. Christianen ◽  
...  
Keyword(s):  

2005 ◽  
Vol 252 (4) ◽  
pp. 1132-1138 ◽  
Author(s):  
Jun Fu ◽  
Yang Cong ◽  
Xiang Yu ◽  
Jian Li ◽  
Caiyuan Pan ◽  
...  
Keyword(s):  

2018 ◽  
Vol 54 (4) ◽  
pp. 401-404 ◽  
Author(s):  
R. Otter ◽  
K. Klinker ◽  
D. Spitzer ◽  
M. Schinnerer ◽  
M. Barz ◽  
...  

ABA′ triblock peptide–polysarcosine–peptide conjugates fold into antiparallel β-sheets, which promotes the self-assembly into polysarcosine-shielded core–shell nanorods with protein repellent properties.


2020 ◽  
Vol 8 (20) ◽  
pp. 4419-4427 ◽  
Author(s):  
Miryam Criado-Gonzalez ◽  
Breyinn Loftin ◽  
Jennifer Rodon Fores ◽  
Dominique Vautier ◽  
Leyla Kocgozlu ◽  
...  

Studying the influence of hydrogel matrices on the self-assembly behavior of peptides and interaction with cells guides the future development of engineered biomaterials.


2019 ◽  
Vol 17 (15) ◽  
pp. 3853-3860 ◽  
Author(s):  
Leixia Mei ◽  
Keming Xu ◽  
Ziran Zhai ◽  
Suyun He ◽  
Tingting Zhu ◽  
...  

Doxorubicin reinforced the self-assembly of RGD-derived peptide conjugates responsive to mild acidity.


Theranostics ◽  
2020 ◽  
Vol 10 (18) ◽  
pp. 8162-8178
Author(s):  
Liu Xu ◽  
Yutong Wang ◽  
Chenqi Zhu ◽  
Shujing Ren ◽  
Yurou Shao ◽  
...  

2020 ◽  
Vol 1219 ◽  
pp. 128587
Author(s):  
Wei Wang ◽  
Zhuoyu Li ◽  
Rong Zeng ◽  
Chunqiang Yang ◽  
Lingbo Ji ◽  
...  

2021 ◽  
Author(s):  
Emerald Taylor ◽  
Akiko Sato ◽  
Prashant Gudeangadi ◽  
David Beal ◽  
James Hopper ◽  
...  

DNA-peptide conjugates offer an opportunity to marry the benefits of both biomolecules, such as the high level of control and programmability found with DNA and the chemical diversity and biological stability of peptides. These hybrid systems offer great potential in fields such as therapeutics, nanotechnology, and robotics to name a few. Using the first DNA-β-turn peptide conjugate, we present three studies designed to investigate the self-assembly of DNA-peptide conjugates over a period of 28 days. Time-course studies, such as these have not been previously conducted for DNA-peptide conjugates, although they are common in pure peptide assembly, for example in amyloid research. By using aging studies to assess the structures produced, we gain insights into the dynamic nature of these systems. The first study explores the influence varying amounts of DNA-peptide conjugates have on the self-assembly of our parent peptide. Study 2 explores how DNA and peptide can work together to change the structures observed during aging. Study 3 investigates the presence of orthogonality within our system by switching the DNA and peptide control on and off independently. These results show that two orthogonal self-assemblies can be combined and operated either independently or in tandem within a single macromolecule, with both spatial and temporal effects upon the resultant nanostructures.


2021 ◽  
Author(s):  
Emerald Taylor ◽  
Akiko Sato ◽  
Prashant Gudeangadi ◽  
David Beal ◽  
James Hopper ◽  
...  

DNA-peptide conjugates offer an opportunity to marry the benefits of both biomolecules, such as the high level of control and programmability found with DNA and the chemical diversity and biological stability of peptides. These hybrid systems offer great potential in fields such as therapeutics, nanotechnology, and robotics to name a few. Using the first DNA-β-turn peptide conjugate, we present three studies designed to investigate the self-assembly of DNA-peptide conjugates over a period of 28 days. Time-course studies, such as these have not been previously conducted for DNA-peptide conjugates, although they are common in pure peptide assembly, for example in amyloid research. By using aging studies to assess the structures produced, we gain insights into the dynamic nature of these systems. The first study explores the influence varying amounts of DNA-peptide conjugates have on the self-assembly of our parent peptide. Study 2 explores how DNA and peptide can work together to change the structures observed during aging. Study 3 investigates the presence of orthogonality within our system by switching the DNA and peptide control on and off independently. These results show that two orthogonal self-assemblies can be combined and operated either independently or in tandem within a single macromolecule, with both spatial and temporal effects upon the resultant nanostructures.


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