Peptide Architecture: Adding an α-Helix to the PYY Lysine Side Chain Provides Nanomolar Binding and Body-Weight-Lowering Effects

ChemMedChem ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. 545-551 ◽  
Author(s):  
Søren L. Pedersen ◽  
Pottayil G. Sasikumar ◽  
Niels Vrang ◽  
Knud J. Jensen
Keyword(s):  
Body Weight ◽  
Side Chain ◽  
Lysine Side Chain ◽  
Α Helix

scholarly journals Cover Picture: Peptide Architecture: Adding an α-Helix to the PYY Lysine Side Chain Provides Nanomolar Binding and Body-Weight-Lowering Effects (ChemMedChem 4/2010)

ChemMedChem ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. 485-485
Author(s):  
Søren L. Pedersen ◽  
Pottayil G. Sasikumar ◽  
Niels Vrang ◽  
Knud J. Jensen
Keyword(s):  
Body Weight ◽  
Side Chain ◽  
Lysine Side Chain ◽  
Α Helix

Catalytic activity of CuGHK peptide-based porous material

2021 ◽  
Author(s):  
Francisco G. Cirujano ◽  
Nuria Martin ◽  
Neyvis Almora-Barrios ◽  
Carlos Martí-Gastaldo
Keyword(s):  
Catalytic Activity ◽  
Porous Material ◽  
Active Sites ◽  
Room Temperature ◽  
Side Chain ◽  
Periodic Distribution ◽  
Lysine Side Chain ◽  
One Step

Room temperature one-step synthesis of the peptide-based porous material with a periodic distribution of pockets decorated with lysine side chain active sites behaves as a heterogeneous organocatalyst. The pockets are...

Stabilising Non-Polar/Polar Side Chain Interactions in the α-Helix

2000 ◽  
Vol 28 (3) ◽  
pp. A72-A72
Author(s):  
Charles D. Andrew ◽  
Simon Penel ◽  
Gareth R. Jones ◽  
Andrew J. Doig
Keyword(s):  
Side Chain ◽  
Α Helix

Structure, stability and folding of the α-helix

2001 ◽  
Vol 68 ◽  
pp. 95-110 ◽  
Author(s):  
Andrew J. Doig ◽  
Charles D. Andrew ◽  
Duncan A. E. Cochran ◽  
Eleri Hughes ◽  
Simon Penel ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Hydrophobic Interactions ◽  
Data Bank ◽  
Site Directed Mutagenesis ◽  
Model Systems ◽  
Side Chain ◽  
Structure Stability ◽  
Helical Peptides ◽  
Vast Number ◽  
Α Helix

Pauling first described the α-helix nearly 50 years ago, yet new features of its structure continue to be discovered, using peptide model systems, site-directed mutagenesis, advances in theory, the expansion of the Protein Data Bank and new experimental techniques. Helical peptides in solution form a vast number of structures, including fully helical, fully coiled and partly helical. To interpret peptide results quantitatively it is essential to use a helix/coil model that includes the stabilities of all these conformations. Our models now include terms for helix interiors, capping, side-chain interactions, N-termini and 310-helices. The first three amino acids in a helix (N1, N2 and N3) and the preceding N-cap are unique, as their amide NH groups do not participate in backbone hydrogen bonding. We surveyed their structures in proteins and measured their amino acid preferences. The results are predominantly rationalized by hydrogen bonding to the free NH groups. Stabilizing side-chain-side-chain energies, including hydrophobic interactions, hydrogen bonding and polar/non-polar interactions, were measured accurately in helical peptides. Helices in proteins show a preference for having approximately an integral number of turns so that their N- and C-caps lie on the same side. There are also strong periodic trends in the likelihood of terminating a helix with a Schellman or αL C-cap motif. The kinetics of α-helix folding have been studied with stopped-flow deep ultraviolet circular dichroism using synchrotron radiation as the light source; this gives a far superior signal-to-noise ratio than a conventional instrument. We find that poly(Glu), poly(Lys) and alanine-based peptides fold in milliseconds, with longer peptides showing a transient overshoot in helix content.

Novel lipid side chain modified exenatide analogs emerged prolonged glucoregulatory activity and potential body weight management properties

2019 ◽  
Vol 27 (20) ◽  
pp. 115070 ◽  
Author(s):  
Chengye Li ◽  
Xingguang Cai ◽  
Yuxuan Dai ◽  
Chunxia Liu ◽  
Xinzhou Bi ◽  
...  
Keyword(s):  
Body Weight ◽  
Weight Management ◽  
Side Chain

scholarly journals LK peptide side chain dynamics at interfaces are independent of secondary structure

2017 ◽  
Vol 19 (42) ◽  
pp. 28507-28511 ◽  
Author(s):  
Michael A. Donovan ◽  
Helmut Lutz ◽  
Yeneneh Y. Yimer ◽  
Jim Pfaendtner ◽  
Mischa Bonn ◽  
...  
Keyword(s):  
Secondary Structure ◽  
Real Time ◽  
Surface Interactions ◽  
Side Chain ◽  
Chain Dynamics ◽  
Air Interface ◽  
Time Observation ◽  
Α Helix ◽  
Side Chain Dynamics ◽  
Real Time Observation

Real-time observation of the ultrafast motions of leucine side chains within model peptides at the water–air interface with representative folds – α-helix, 310-helix, β-strand – show that interfacial dynamics are mostly determined by surface interactions.

scholarly journals Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array

2012 ◽  
Vol 134 (17) ◽  
pp. 7317-7320 ◽  
Author(s):  
Lisa M. Johnson ◽  
David E. Mortenson ◽  
Hyun Gi Yun ◽  
W. Seth Horne ◽  
Thomas J. Ketas ◽  
...  
Keyword(s):  
Side Chain ◽  
Α Helix

L-Lysine sulphate, C6H16N2O22+.SO42−: a novel conformation of the L-lysine side chain

1983 ◽  
Vol 39 (2) ◽  
pp. 281-283 ◽  
Author(s):  
S. Capasso ◽  
C. A. Mattia ◽  
L. Mazzarella ◽  
A. Zagari
Keyword(s):  
Side Chain ◽  
Lysine Side Chain
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