Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Celen Cenker"'
Publikováno v:
Langmuir. 30:10072-10079
We compare the aqueous self-assembly behavior within the homologous peptide series A(n)K, where A is alanine, K is lysine, and n = 4, 6, 8, and 10. The aqueous peptide solubility, phi(s) (volume fraction), depends strongly on the number of hydrophobi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::71918a7e48167123f89c47e6b2d12f47
https://doi.org/10.1021/la5016324
https://doi.org/10.1021/la5016324
Publikováno v:
Langmuir. 25:4262-4265
The self-assembly of the trifluoroacetate salt of the short peptide (ala)6-lys (A6K) in water has been investigated by cryo-transmission electron microscopy and small-angle X-ray scattering. For concentrations below ca. 12%, the peptide does not self
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f8c280c173433dcbe28e1f34ed889b4
https://doi.org/10.1021/la804175h
https://doi.org/10.1021/la804175h
Autor:
Paul H. H. Bomans, Celen Cenker, Burcu Dedeoglu, Heiner Friedrich, Nico A. J. M. Sommerdijk, Viktorya Aviyente, Seyda Bucak, Ulf Olsson
Publikováno v:
Soft Matter, 8(28), 7463-7470. Royal Society of Chemistry
Above its critical aggregation concentration the tfa salt of the peptide A6K self-assembles into micron long, hollow nanotubes with uniform diameters of 52 nm and crystalline order. Here we combine the use of SAXS with cryoTEM and cryo-electron tomog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31518a2b73ef78ee224b080795ab815f
https://research.tue.nl/nl/publications/4c65979c-98c1-4f9e-b486-e09e35c844ba
https://research.tue.nl/nl/publications/4c65979c-98c1-4f9e-b486-e09e35c844ba
Autor:
Beatriu Escuder, Ian W. Hamley, Valeria Castelletto, Juan F. Miravet, Raffaele Mezzenga, Celen Cenker, Ulf Olsson, Francisco Rodríguez-Llansola, Jozef Adamcik
Publikováno v:
The journal of physical chemistry. B. 115(9)
The influence of charge and aromatic stacking interactions on the self-assembly of a series of four model amyloid peptides has been examined. The four model peptides are based on the KLVFF motif from the amyloid beta peptide, A beta(16-20) extended a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc4cbfc29e03048b448d97e32131e322
https://pubmed.ncbi.nlm.nih.gov/21309578
https://pubmed.ncbi.nlm.nih.gov/21309578
Publikováno v:
Langmuir : the ACS journal of surfaces and colloids. 26(14)
A micellar nanocontainer delivery and release system is designed on the basis of a peptide-polymer conjugate. The hybrid molecules self-assemble into micelles comprising a modified amyloid peptide core surrounded by a PEG corona. The modified amyloid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dcdfbe33dfaef64fe01318a7a54742df
https://pubmed.ncbi.nlm.nih.gov/20666427
https://pubmed.ncbi.nlm.nih.gov/20666427
Publikováno v:
The journal of physical chemistry. B. 114(23)
We study the effects of NaCl on the self-assembly of AAKLVFF and beta A beta AKLVFF in solution. Both AAKLVFF and beta A beta AKLVFF self-assemble into twisted fibers in aqueous solution. The addition of NaCl to aqueous solutions of AAKLVFF produces
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1b34408b0e164859d759d6ef3e4693c6
https://pubmed.ncbi.nlm.nih.gov/20496898
https://pubmed.ncbi.nlm.nih.gov/20496898
Publikováno v:
Soft Matter. 7:4868
The trifluoroacetate (tfa) salt of the peptide (ala)6lys self-assembles in water into very long, hollow nanotubes with a radius R = 26 nm, above a critical aggregation concentration (volume fraction), cac = 0.10. The peptides carry a net positive cha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0f431e56b04842aa03fb99d6fe22683
https://doi.org/10.1039/c0sm01186j
https://doi.org/10.1039/c0sm01186j
Publikováno v:
Chemical Communications. 46:6270
The structure of single wall peptide nanotubes is presented for the model surfactant-like peptide A6K. Capillary flow alignment of a sample in the nematic phase at high concentration in water leads to oriented X-ray diffraction patterns. Analysis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e071b73234e3ea12c6438048dc3c1f05
https://doi.org/10.1039/c0cc00212g
https://doi.org/10.1039/c0cc00212g