ChemInform Abstract: Formation of Dihydropyridone- and Pyridone-Based Peptide Analogues Through Aza-Annulation of β-Enamino Ester and Amide Substrates with α-Amido Acrylate Derivatives.

ChemInform ◽  
2010 ◽  
Vol 28 (27) ◽  
pp. no-no
Author(s):  
L. G. BEHOLZ ◽  
P. BENOVSKY ◽  
D. L. WARD ◽  
N. S. BARTA ◽  
J. R. STILLE
Keyword(s):  
Peptide Analogues

IMMUNOGENICITY OF HEPATITIS B SURFACE ANTIGEN SYNTHETIC PEPTIDE ANALOGUES

1987 ◽  
pp. 565-568
Author(s):  
B. Lammek ◽  
G. Kupryszewski ◽  
U. Ragnarsson ◽  
H. Świderska ◽  
M. Jastrzebska ◽  
...  
Keyword(s):  
Hepatitis B ◽  
Surface Antigen ◽  
Synthetic Peptide ◽  
Hepatitis B Surface Antigen ◽  
Peptide Analogues

Positive charge modifications alter the ability of XIP to inhibit the plasma membrane calcium pump

1996 ◽  
Vol 271 (3) ◽  
pp. C736-C741 ◽  
Author(s):  
W. Xu ◽  
C. Gatto ◽  
M. A. Milanick
Keyword(s):  
Plasma Membrane ◽  
Positive Charge ◽  
Calcium Pump ◽  
Inhibitory Peptide ◽  
Ca Pump ◽  
Contact Points ◽  
Plasma Membrane Calcium Pump ◽  
Peptide Analogues ◽  
Positively Charged

Exchange inhibitory peptide (XIP; RRLLFYKYVYKRYRAGKQRG) is the shortest peptide that inhibits the plasma membrane Ca pump at high Ca (A. Enyedi, T. Vorherr, P. James, D. J. McCormick, A. G. Filoteo, E. Carafoli, and J. T. Penniston, J. Biol. Chem. 264: 12313-12321, 1989). Sulfosuccinimidyl acetate (SNA)-modified XIP does not inhibit the Ca pump; SNA neutralizes the positive charge on Lys at positions 7, 11, and 17. Peptide 2CK-XIP (RRLLFYRYVYRCYCAGRQKG) inhibits the pump, but the iodoacetamido-modified peptide does not inhibit. Three peptide analogues, in which 7, 11, and 17 were Ala, Cys, or Lys, inhibited about as well as XIP. SNA modification of these analogues (each with 1 Lys) did not inhibit. SNA modification of 2CK-XIP results in a peptide that does not inhibit; thus position 19 is important. Our results suggest that it is critical that position 19 be positively charged, that positions 7, 11, and 17 are important contact points between XIP and the Ca pump (with at least one positively charged), and that, whereas it is not essential that residues 12 and 14 be positive, they cannot be negative.

Improving the Tumor Uptake of 99mTc-Labeled Neuropeptides Using Stabilized Peptide Analogues

2004 ◽  
Vol 19 (2) ◽  
pp. 181-188 ◽  
Author(s):  
Peter Bläuenstein ◽  
Elisa García Garayoa ◽  
Dominique Rüegg ◽  
Alain Blanc ◽  
Dirk Tourwé ◽  
...  
Keyword(s):  
Tumor Uptake ◽  
Peptide Analogues

Design of Peptide Analogues with Improved Activity Using a Novel de Novo Protein Design Approach

2004 ◽  
Vol 43 (14) ◽  
pp. 3817-3826 ◽  
Author(s):  
J. L. Klepeis ◽  
C. A. Floudas ◽  
D. Morikis ◽  
C. G. Tsokos ◽  
J. D. Lambris
Keyword(s):  
Protein Design ◽  
De Novo ◽  
Design Approach ◽  
De Novo Protein Design ◽  
Peptide Analogues

Cationicity and hydrophobicity enhance the cytotoxic potency of Phoratoxin C anticancer peptide analogues against triple negative breast cancer cells

2021 ◽  
Vol 17 ◽  
Author(s):  
Chu Xin Ng ◽  
Cheng Foh Le ◽  
Sau Har Lee
Keyword(s):  
Cancer Cells ◽  
Anticancer Agents ◽  
Breast Cancer Cells ◽  
Critical Role ◽  
Three Dimensional ◽  
Vero Cells ◽  
Anticancer Peptides ◽  
Α Helix ◽  
Peptide Analogues

Background: Anticancer peptides (ACPs) have received increasing attention as a promising class of novel anticancer agents owing to its potent and rapid cytotoxic properties. In this study, we aim to investigate the effects of cationicity and hydrophobicity in modulating the cytotoxicity of PtxC, a class of ACP from the leafy mistletoe Phoradendron tomentosum against the MDA-MB-231 and Vero cells. Method: We designed a series of four PtxC analogues (PA1 – PA4) by residual substitutions with specific amino acids to introduce the specific charge and hydrophobicity alterations to the analogues. The cytotoxicity strength of the PtxC analogues on MDA-MB-231 and Vero cells were tested by using MTT assay at 24 hours post treatment. Results: PA1, PA2 and PA4 displayed marked increases in cytotoxicity against both MDA-MB-231 and Vero cells and can be ranked in the order of PA2 > PA4 > PA1 > PtxC > PA3. Sequence-activity relationship analyses of the designed analogues showed that an increase in the level of cationicity and hydrophobicity correlated well with the enhanced cytotoxic activity of PtxC analogues. This was observed with PA1 (netC +8) and PA2 (netC +10) in comparison to PtxC (netC +7). Similar finding was observed for PA4 (GRAVY +0.070) in contrast to PtxC (GRAVY -0.339). Three-dimensional modelling predicted a double α-helix structure in PtxC class of ACP. The larger first helix in PA2 and PA4 was suggested to be responsible for the enhanced cytotoxicity observed. Conclusion: The critical role of cationicity and hydrophobicity in enhancing cytotoxicity of PtxC class of ACPs were clearly demonstrated in our study. The current findings could be extrapolated to benefit peptide design strategy in other classes of ACPs toward the discovery of highly potent ACPs against cancer cells as potential novel therapeutic agents.

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