83537-94-4Relevant articles and documents
Helical Peptides Design for Molecular Dipoles Functionalization of Wide Band Gap Oxides
Bartynski, Robert A.,Chen, Yuan,Galoppini, Elena,Harmer, Ryan,Rangan, Sylvie,Viereck, Jonathan
supporting information, p. 3489 - 3498 (2020/03/06)
The use of helical hexapeptides to establish a surface dipole layer on a TiO2 substrate, with the goal of influencing the energy levels of a coadsorbed chromophore, is explored. Two helical hexapeptides, synthesized from 2-amino isobutyric acid
Conformation-specific spectroscopy of capped, gas-phase Aib oligomers: Tests of the Aib residue as a 310-helix former
Gord, Joseph R.,Hewett, Daniel M.,Hernandez-Castillo, Alicia O.,Blodgett, Karl N.,Rotondaro, Matthew C.,Varuolo, Adalgisa,Kubasik, Matthew A.,Zwier, Timothy S.
, p. 25512 - 25527 (2016/09/23)
The conformational preferences of a series of capped peptides containing the helicogenic amino acid aminoisobutyric acid (Aib) (Z-Aib-OH, Z-(Aib)2-OMe, and Z-(Aib)4-OMe) are studied in the gas phase under expansion-cooled conditions. Aib oligomers are known to form 310-helical secondary structures in solution and in the solid phase. However, in the gas phase, accumulation of a macrodipole as the helix grows could inhibit helix stabilization. Implementing single-conformation IR spectroscopy in the NH stretch region, Z-Aib-OH and Z-(Aib)2-OMe are both observed to have minor conformations that exhibit dihedral angles consistent with the 310-helical portion of the Ramachandran map (φ, ψ = -57°, -30°), even though they lack sufficient backbone length to form 10-membered rings which are a hallmark of the developed 310-helix. For Z-(Aib)4-OMe three conformers are observed in the gas phase. Single-conformation infrared spectroscopy in both the NH stretch (Amide A) and CO stretch (Amide I) regions identifies the main conformer as an incipient 310-helix, having two free NH groups and two C10 H-bonded NH groups, labeled an F-F-10-10 structure, with a calculated dipole moment of 13.7 D. A second minor conformer has an infrared spectrum characteristic of an F-F-10-7 structure in which the third and fourth Aib residues have φ, ψ = 75°, -74° and -52°, 143°, Ramachandran angles which fall outside of the typical range for 310-helices, and a dipole moment that shrinks to 5.4 D. These results show Aib to be a 310-helix former in the gas phase at the earliest stages of oligomer growth.
Deracemization and the first CD spectrum of a 310-helical peptide made of achiral α-amino-isobutyric acid residues in a chiral membrane mimetic environment
Ceccacci, Francesca,Mancini, Giovanna,Rossi, Paola,Scrimin, Paolo,Sorrenti, Alessandro,Tecilla, Paolo
, p. 10133 - 10135 (2013/10/22)
Interaction of the racemic helical homo-octapeptide made by the achiral Cα-methyl alanine (Aib) amino acid with a chiral enantiopure micellar aggregate made of N-dodecylproline led to the deracemization of the helical Aib sequence thus allowing
Peptide fragment coupling using a continuous-flow photochemical rearrangement of nitrones
Zhang, Yuan,Blackman, Melissa L.,Leduc, Andrew B.,Jamison, Timothy F.
, p. 4251 - 4255 (2013/05/08)
Go with the flow: A general approach for amide bond formation by way of a continuous-flow photochemical rearrangement of nitrones was described (see scheme). Simple aryl-alkyl amide bonds as well as complex peptide bonds were constructed efficiently with a residence time less than 20minutes. A tetrapeptide was synthesized in this way and the method could be applied to peptide fragment coupling. Copyright
Rational design of gold(III)-dithiocarbamato peptidomimetics for the targeted anticancer chemotherapy
Kouodom, Morelle Negom,Boscutti, Giulia,Celegato, Marta,Crisma, Marco,Sitran, Sergio,Aldinucci, Donatella,Formaggio, Fernando,Ronconi, Luca,Fregona, Dolores
, p. 248 - 260 (2013/01/15)
As a further extension of our research work focusing on the development of gold(III)-dithiocarbamato dtc derivatives of oligopeptides as potential anticancer agents, complexes [AuIIIX2(dtc-Sar-l-Ser(t-Bu)- O(t-Bu))] (X = Br (1a)/Cl (
Emerimicins III and IV and their ethylalanine12 epimers. Facilitated chemical-enzymatic synthesis and a qualitative evaluation of their solution structures
Slomczynska, Urszula,Beusen, Denise D.,Zabrocki, Janusz,Kociolek, Karol,Redlinski, Adam,Rensser, Fritz,Hutton, William C.,Leplawy, Miroslaw T.,Marshall, Garland R.
, p. 4095 - 4106 (2007/10/02)
The peptaibol antibiotics, emerimicin III and IV (Ac-Phe1-MeA2-MeA3-MeA4-VaI 5-Gly6-Leu7-MeA8-MeA 9-Hyp10-Gln11-R-EtA12-Hyp
Determination of an 8-? interatomic distance in a helical peptide by solid-state NMR spectroscopy
Holl, Susan M.,Marshall, Garland R.,Beusen, Denise D.,Kociolek, Karol,Redlinski, Adam S.,Leplawy, Miroslaw T.,McKay, Robert A.,Vega, Shimon,Schaefer, Jacob
, p. 4830 - 4833 (2007/10/02)
The combination of transferred-echo double resonance (TEDOR) with rotational-echo double resonance (REDOR) has been used to measure an 8-? fluorine-carbon internuclear distance in a nine-residue fragment of the peptide antibiotic emerimicin. The fragment is 19FCH2CO-Phe-MeA-MeA-[1-13C]MeA-[ 15N]Val-Gly-Leu-MeA-MeA-OBzl (MeA = α-methylalanine or aminoisobutyric acid). The TEDOR part of this magic-angle-spinning, solid-state NMR experiment selects the 13C label by its dipolar coupling to 15N and suppresses the natural-abundance carbon background. The REDOR part of the experiment measures dipolar coupling of the selected carbon to 19F. The TEDOR-REDOR combined experiment works with a variety of spin 1/2 nuclei and can be used to characterize internuclear distances and geometry in macromolecular aggregates that do not crystallize.
SYNTHESE VON 2-METHYLALANIN-PEPTIDEN, DIE pH-ABHAENGIGKEIT IHRER 13C-NMR-SPECTREN UND EINE NEUE METHODE ZUR AUSWERTUNG UEBER CS-DIAGRAMME
Leibfritz, Dieter,Haupt, Erhard,Dubischar, Norbert,Lachmann, Heinrich,Oekonomopulos, Raymond,Jung, Guenther
, p. 2165 - 2182 (2007/10/02)
The uncommon amino-acid 2-methylalanine (α-aminoisobutiryc acid, Aib) was investigated by 13C-NMR.The chemical shifts of amino- or carboxy-protected derivates of Aib and of protected oligopeptides are discussed with respect to neighbouring groups and amino acids.The pH-dependence of the 13C-NMR spectra of Aib, Aib-Ala, Ala-Aib, Aib-Ala-Aib and Aib-Ala-Aib-Ala-Aib was studied.Using these examples, a new and advantageous method is demonstrated for the first time for the evaluation of NMR titration curves, which uses so-called chemical shift diagrams (CS diagrams).