-
1
-
-
0032877184
-
Therapeutic peptides revisited
-
Latham P.W. Therapeutic peptides revisited. Nat Biotechnol. 17:1999;755-757.
-
(1999)
Nat Biotechnol
, vol.17
, pp. 755-757
-
-
Latham, P.W.1
-
2
-
-
0542421525
-
Foldamers: A manifesto
-
Gellman S.H. Foldamers: a manifesto. Acc Chem Res. 31:1998;173-180.
-
(1998)
Acc Chem Res
, vol.31
, pp. 173-180
-
-
Gellman, S.H.1
-
4
-
-
0032705431
-
Bioinspired polymeric materials: In-between proteins and plastics
-
Barron A.E., Zuckermann R.N. Bioinspired polymeric materials: in-between proteins and plastics. Curr Opin Chem Biol. 3:1999;681-687.
-
(1999)
Curr Opin Chem Biol
, vol.3
, pp. 681-687
-
-
Barron, A.E.1
Zuckermann, R.N.2
-
5
-
-
0035896429
-
Innate immunity: Ancient system gets new respect
-
Gura T. Innate immunity: ancient system gets new respect. Science. 291:2001;2068-2071.
-
(2001)
Science
, vol.291
, pp. 2068-2071
-
-
Gura, T.1
-
6
-
-
0037165196
-
Antimicrobial peptides of multicellular organisms
-
Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 415:2002;389-395.
-
(2002)
Nature
, vol.415
, pp. 389-395
-
-
Zasloff, M.1
-
7
-
-
0033864862
-
Amphipathic, α-helical antimicrobial peptides
-
A comprehensive review of the most common class of antibacterial peptides. The natural sources of these peptides are described. Additionally, the mode of action and physical characteristics responsible for activities are discussed, in detail.
-
Tossi A., Sandri L., Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers. 55:2000;4-30. A comprehensive review of the most common class of antibacterial peptides. The natural sources of these peptides are described. Additionally, the mode of action and physical characteristics responsible for activities are discussed, in detail.
-
(2000)
Biopolymers
, vol.55
, pp. 4-30
-
-
Tossi, A.1
Sandri, L.2
Giangaspero, A.3
-
8
-
-
0032443219
-
Mode of action of linear amphipathic α-helical antimicrobial peptides
-
Oren Z., Shai Y. Mode of action of linear amphipathic α-helical antimicrobial peptides. Biopolymers. 47:1998;451-463.
-
(1998)
Biopolymers
, vol.47
, pp. 451-463
-
-
Oren, Z.1
Shai, Y.2
-
9
-
-
0025189536
-
Interactions between Salmonella typhimurium lipopolysaccharide and the antimicrobial peptide, magainin 2 amide
-
Rana F.R., Sultany C.M., Blazyk J. Interactions between Salmonella typhimurium lipopolysaccharide and the antimicrobial peptide, magainin 2 amide. FEBS Lett. 261:1990;464-467.
-
(1990)
FEBS Lett
, vol.261
, pp. 464-467
-
-
Rana, F.R.1
Sultany, C.M.2
Blazyk, J.3
-
10
-
-
0031058903
-
Modulation of magainin-2-lipid bilayer interactions by peptide charge
-
Matsuzaki K., Nakamura A., Murase O., Sugishita K.I., Fujii N., Miyaji K. Modulation of magainin-2-lipid bilayer interactions by peptide charge. Biochemistry. 36:1997;2104-2111.
-
(1997)
Biochemistry
, vol.36
, pp. 2104-2111
-
-
Matsuzaki, K.1
Nakamura, A.2
Murase, O.3
Sugishita, K.I.4
Fujii, N.5
Miyaji, K.6
-
11
-
-
0030981655
-
Structure and functions of channel-forming peptides: Magainins, cecropins, melittin, and alamethicin
-
Bechinger B. Structure and functions of channel-forming peptides: magainins, cecropins, melittin, and alamethicin. J Membr Biol. 156:1997;197-211.
-
(1997)
J Membr Biol
, vol.156
, pp. 197-211
-
-
Bechinger, B.1
-
12
-
-
2042513493
-
Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
-
Zasloff M. Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA. 84:1987;5449-5453.
-
(1987)
Proc Natl Acad Sci USA
, vol.84
, pp. 5449-5453
-
-
Zasloff, M.1
-
13
-
-
0035471135
-
β-Peptides: From structure to function
-
This review is an excellent summary of the documented secondary structures adopted by β-peptides, and how primary sequence ultimately dictates folded conformation in these oligomers.
-
Cheng R.P., Gellman S.H., DeGrado W.F. β-Peptides: from structure to function. Chem Rev. 101:2001;3219-3232. This review is an excellent summary of the documented secondary structures adopted by β-peptides, and how primary sequence ultimately dictates folded conformation in these oligomers.
-
(2001)
Chem Rev
, vol.101
, pp. 3219-3232
-
-
Cheng, R.P.1
Gellman, S.H.2
DeGrado, W.F.3
-
15
-
-
0030995823
-
Residue-based control of helix shape in β-peptide oligomers
-
Appella D.H., Christianson L.A., Klein D.A., Powell D.R., Huang X., Joseph J., Barchi J., Gellman S.H. Residue-based control of helix shape in β-peptide oligomers. Nature. 387:1997;381-384.
-
(1997)
Nature
, vol.387
, pp. 381-384
-
-
Appella, D.H.1
Christianson, L.A.2
Klein, D.A.3
Powell, D.R.4
Huang, X.5
Joseph, J.6
Barchi, J.7
Gellman, S.H.8
-
17
-
-
0034802565
-
De novo design, synthesis, and characterization of antimicrobial β-peptides
-
Liu D., DeGrado W.F. De novo design, synthesis, and characterization of antimicrobial β-peptides. J Am Chem Soc. 123:2001;7553-7559.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 7553-7559
-
-
Liu, D.1
DeGrado, W.F.2
-
18
-
-
0035496146
-
On the antimicrobial and hemolytic activities of amphiphilic β-peptides
-
Arvidsson P.I., Frackenpohl J., Ryder N.S., Liechty B., Petersen F., Zimmermann H., Camenisch G.P., Woessner R., Seebach D. On the antimicrobial and hemolytic activities of amphiphilic β-peptides. ChemBioChem. 2:2001;771-773.
-
(2001)
ChemBioChem
, vol.2
, pp. 771-773
-
-
Arvidsson, P.I.1
Frackenpohl, J.2
Ryder, N.S.3
Liechty, B.4
Petersen, F.5
Zimmermann, H.6
Camenisch, G.P.7
Woessner, R.8
Seebach, D.9
-
19
-
-
17344384874
-
Non-haemolytic β-amino-acid oligomers
-
This letter is the first report of a non-haemolytic β-peptide antibacterial peptide mimic, named 'β-17'. In contrast to DeGrado's work, which employed the 14-helix, β-17 adopts a 12-helix.
-
Porter E.A., Wang X., Lee H.-S., Weisblum B., Gellman S.H. Non-haemolytic β-amino-acid oligomers. Nature. 404:2000;565. This letter is the first report of a non-haemolytic β-peptide antibacterial peptide mimic, named 'β-17'. In contrast to DeGrado's work, which employed the 14-helix, β-17 adopts a 12-helix.
-
(2000)
Nature
, vol.404
, pp. 565
-
-
Porter, E.A.1
Wang, X.2
Lee, H.-S.3
Weisblum, B.4
Gellman, S.H.5
-
20
-
-
0037134881
-
Tolerance of acyclic residues in the β-peptide 12-helix: Access to diverse side-chain arrays for biological applications
-
LePlae P.R., Fisk J.D., Porter E.A., Weisblum B., Gellman S.H. Tolerance of acyclic residues in the β-peptide 12-helix: access to diverse side-chain arrays for biological applications. J Am Chem Soc. 124:2002;6820-6821.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 6820-6821
-
-
LePlae, P.R.1
Fisk, J.D.2
Porter, E.A.3
Weisblum, B.4
Gellman, S.H.5
-
21
-
-
0037178109
-
Mimicry of host-defense peptides by unnatural oligomers: Antimicrobial β-peptides
-
This is the first detailed study of how physical parameters of helical β-peptide antibacterial compounds affect antibacterial and haemolytic efficacy. The results mirror those found for antibacterial α-peptides; facial amphipathicity, as well as a precise ratio of hydrophobic to charged residues, is required for optimal activity.
-
Porter E.A., Weisblum B., Gellman S.H. Mimicry of host-defense peptides by unnatural oligomers: antimicrobial β-peptides. J Am Chem Soc. 124:2002;7324-7330. This is the first detailed study of how physical parameters of helical β-peptide antibacterial compounds affect antibacterial and haemolytic efficacy. The results mirror those found for antibacterial α-peptides; facial amphipathicity, as well as a precise ratio of hydrophobic to charged residues, is required for optimal activity.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 7324-7330
-
-
Porter, E.A.1
Weisblum, B.2
Gellman, S.H.3
-
22
-
-
0037202210
-
Structure-activity studies of 14-helical antimicrobial β-peptides: Probing the relationship between conformational stability and antimicrobial potency
-
e-pub ahead of print: DOI10.1021/ja027042
-
Raguse TL, Porter EA, Weisblum B, Gellman SH: Structure-activity studies of 14-helical antimicrobial β-peptides: probing the relationship between conformational stability and antimicrobial potency. J Am Chem Soc 2002, e-pub ahead of print: DOI10.1021/ja027042.
-
(2002)
J Am Chem Soc
-
-
Raguse, T.L.1
Porter, E.A.2
Weisblum, B.3
Gellman, S.H.4
-
23
-
-
0037014693
-
New poly(phenyleneethynylene)s with cationic, facially amphipathic structures
-
Arnt L., Tew G.N. New poly(phenyleneethynylene)s with cationic, facially amphipathic structures. J Am Chem Soc. 124:2002;7664-7665.
-
(2002)
J Am Chem Soc
, vol.124
, pp. 7664-7665
-
-
Arnt, L.1
Tew, G.N.2
-
24
-
-
84962436408
-
Hydrazino peptides as foldamers: An extension of the β-peptide concept
-
Günther R., Hofmann H.-J. Hydrazino peptides as foldamers: an extension of the β-peptide concept. J Am Chem Soc. 123:2001;247-255.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 247-255
-
-
Günther, R.1
Hofmann, H.-J.2
-
25
-
-
0026726041
-
Peptoids: A modular approach to drug discovery
-
Simon R.J., Kania R.S., Zuckermann R.N., Huebner V.D., Jewell D.A., Banville S., Ng S., Wang L., Rosenberg S., Marlowe C.K., et al. Peptoids: a modular approach to drug discovery. Proc Natl Acad Sci USA. 89:1992;9367-9371.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 9367-9371
-
-
Simon, R.J.1
Kania, R.S.2
Zuckermann, R.N.3
Huebner, V.D.4
Jewell, D.A.5
Banville, S.6
Ng, S.7
Wang, L.8
Rosenberg, S.9
Marlowe, C.K.10
-
26
-
-
0034835809
-
Peptoid oligomers with α-chiral, aromatic side chains: Sequence requirements for the formation of stable peptoid helices
-
Wu C., Sanborn T., Huang K., Zuckermann R., Barron A. Peptoid oligomers with α-chiral, aromatic side chains: sequence requirements for the formation of stable peptoid helices. J Am Chem Soc. 123:2001;6778-6784.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 6778-6784
-
-
Wu, C.1
Sanborn, T.2
Huang, K.3
Zuckermann, R.4
Barron, A.5
-
27
-
-
0034822676
-
Peptoid oligomers with α-chiral, aromatic side chains: Effects of chain length on secondary structure
-
Wu C.W., Sanborn T.J., Zuckermann R.N., Barron A.E. Peptoid oligomers with α-chiral, aromatic side chains: effects of chain length on secondary structure. J Am Chem Soc. 123:2001;2958-2963.
-
(2001)
J Am Chem Soc
, vol.123
, pp. 2958-2963
-
-
Wu, C.W.1
Sanborn, T.J.2
Zuckermann, R.N.3
Barron, A.E.4
-
28
-
-
0036143238
-
Extreme stability of helices formed by water-soluble poly-N-substituted glycines (polypeptoids) with α-chiral side chains
-
This article describes an amphiphilic, water-soluble 36-mer peptoid with unusually stable secondary structure. Studies by circular dichroism suggest that this peptoid retains helical structure at temperatures of at least 75°C and in 8 M aqueous urea. These results support the view that steric repulsion is the primary force stabilizing peptoid secondary structure.
-
Sanborn T., Wu C., Zuckermann R., Barron A. Extreme stability of helices formed by water-soluble poly-N-substituted glycines (polypeptoids) with α-chiral side chains. Biopolymers. 63:2002;12-20. This article describes an amphiphilic, water-soluble 36-mer peptoid with unusually stable secondary structure. Studies by circular dichroism suggest that this peptoid retains helical structure at temperatures of at least 75°C and in 8 M aqueous urea. These results support the view that steric repulsion is the primary force stabilizing peptoid secondary structure.
-
(2002)
Biopolymers
, vol.63
, pp. 12-20
-
-
Sanborn, T.1
Wu, C.2
Zuckermann, R.3
Barron, A.4
-
29
-
-
0000908874
-
Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis
-
Zuckermann R.N., Kerr J.M., Kent S.B.H., Moos W.H. Efficient method for the preparation of peptoids [oligo(N-substituted glycines)] by submonomer solid-phase synthesis. J Am Chem Soc. 114:1992;10646-10647.
-
(1992)
J Am Chem Soc
, vol.114
, pp. 10646-10647
-
-
Zuckermann, R.N.1
Kerr, J.M.2
Kent, S.B.H.3
Moos, W.H.4
-
30
-
-
0029059507
-
Comparison of the proteolytic susceptibilities of homologous L-amino acid, D-amino acid, and N-substituted glycine peptide and peptoid oligomers
-
Miller S.M., Simon R.J., Ng S., Zuckermann R.N., Kerr J.M., Moos W.H. Comparison of the proteolytic susceptibilities of homologous L-amino acid, D-amino acid, and N-substituted glycine peptide and peptoid oligomers. Drug Dev Res. 35:1995;20-32.
-
(1995)
Drug Dev Res
, vol.35
, pp. 20-32
-
-
Miller, S.M.1
Simon, R.J.2
Ng, S.3
Zuckermann, R.N.4
Kerr, J.M.5
Moos, W.H.6
-
31
-
-
0037117538
-
De novo design of biomimetic antimicrobial polymers
-
This paper reports the synthesis of a series of facially amphiphilic polyacrylamides that exhibit good antibacterial activity, but significant hemolysis. These polymers provide a cheaper, more easily synthesized alternative to the previously synthesized β-peptide magainin mimics.
-
Tew G.N., Liu D., Chen B., Doerksen R.J., Kaplan J., Carroll P.J., Klein M.L., DeGrado W.F. De novo design of biomimetic antimicrobial polymers. Proc Natl Acad Sci USA. 99:2002;5110-5114. This paper reports the synthesis of a series of facially amphiphilic polyacrylamides that exhibit good antibacterial activity, but significant hemolysis. These polymers provide a cheaper, more easily synthesized alternative to the previously synthesized β-peptide magainin mimics.
-
(2002)
Proc Natl Acad Sci USA
, vol.99
, pp. 5110-5114
-
-
Tew, G.N.1
Liu, D.2
Chen, B.3
Doerksen, R.J.4
Kaplan, J.5
Carroll, P.J.6
Klein, M.L.7
DeGrado, W.F.8
-
32
-
-
0028290825
-
Control of RNA initiation and elongation at the HIV-1 promoter
-
Jones K.A., Peterlin B.M. Control of RNA initiation and elongation at the HIV-1 promoter. Annu Rev Biochem. 63:1994;717-743.
-
(1994)
Annu Rev Biochem
, vol.63
, pp. 717-743
-
-
Jones, K.A.1
Peterlin, B.M.2
-
33
-
-
0033599370
-
High affinity and specific binding of HIV-1 TAR RNA by a Tat-derived oligourea
-
Tamilarasu N., Huq I., Rana T.M. High affinity and specific binding of HIV-1 TAR RNA by a Tat-derived oligourea. J Am Chem Soc. 121:1999;1597-1598.
-
(1999)
J Am Chem Soc
, vol.121
, pp. 1597-1598
-
-
Tamilarasu, N.1
Huq, I.2
Rana, T.M.3
-
34
-
-
0031561062
-
HIV-1 TAR RNA recognition by an unnatural biopolymer
-
Wang X., Huq I., Rana T. HIV-1 TAR RNA recognition by an unnatural biopolymer. J Am Chem Soc. 119:1997;6444-6445.
-
(1997)
J Am Chem Soc
, vol.119
, pp. 6444-6445
-
-
Wang, X.1
Huq, I.2
Rana, T.3
-
35
-
-
0035952281
-
Targetting RNA with peptidomimetic oligomers in human cells
-
This article summarizes the development of oligourea and oligocarbamate mimetics of residues 48-57 of HIV-1 Tat protein. These oligomers were found to inhibit HIV gene expression in HeLa cells.
-
Tamilarasu N., Huq I., Rana T.M. Targetting RNA with peptidomimetic oligomers in human cells. Bioorg Med Chem Lett. 11:2001;505-507. This article summarizes the development of oligourea and oligocarbamate mimetics of residues 48-57 of HIV-1 Tat protein. These oligomers were found to inhibit HIV gene expression in HeLa cells.
-
(2001)
Bioorg Med Chem Lett
, vol.11
, pp. 505-507
-
-
Tamilarasu, N.1
Huq, I.2
Rana, T.M.3
-
36
-
-
0024262589
-
Cellular uptake of the Tat protein from human immunodeficiency virus
-
Frankel A.D., Pabo C.O. Cellular uptake of the Tat protein from human immunodeficiency virus. Cell. 55:1988;1189-1193.
-
(1988)
Cell
, vol.55
, pp. 1189-1193
-
-
Frankel, A.D.1
Pabo, C.O.2
-
37
-
-
0030904245
-
A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
-
Vivès E., Brodin P., Lebleu B. A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J Biol Chem. 272:1997;16010-16017.
-
(1997)
J Biol Chem
, vol.272
, pp. 16010-16017
-
-
Vivès, E.1
Brodin, P.2
Lebleu, B.3
-
38
-
-
0034700141
-
The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
-
Wender P.A., Mitchell D.J., Pelkey E.T., Steinman L., Rothbard J.B. The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc Natl Acad Sci USA. 97:2000;13003-13008.
-
(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 13003-13008
-
-
Wender, P.A.1
Mitchell, D.J.2
Pelkey, E.T.3
Steinman, L.4
Rothbard, J.B.5
-
40
-
-
0035950179
-
Utility of azapeptides as major histocompatibility complex class II protein ligands for T-cell activation
-
Hart M., Beeson C. Utility of azapeptides as major histocompatibility complex class II protein ligands for T-cell activation. J Med Chem. 44:2001;3700-3709.
-
(2001)
J Med Chem
, vol.44
, pp. 3700-3709
-
-
Hart, M.1
Beeson, C.2
-
41
-
-
0036009892
-
Major histocompatibility complex class II binding characteristics of peptoid-peptide hybrids
-
Haan Ecd, Wauben M.H.M., Grosfeld-Stulemeyer M.C., Kruijtzer J.A.W., Liskamp R.M.J., Moret E.E. Major histocompatibility complex class II binding characteristics of peptoid-peptide hybrids. Bioorg Med Chem. 10:2002;1939-1945.
-
(2002)
Bioorg Med Chem
, vol.10
, pp. 1939-1945
-
-
Haan Ecd1
Wauben, M.H.M.2
Grosfeld-Stulemeyer, M.C.3
Kruijtzer, J.A.W.4
Liskamp, R.M.J.5
Moret, E.E.6
-
42
-
-
0031857028
-
Design, synthesis, and biological activities of potent and selective somatostatin analogues incorporating novel peptoid residues
-
Tran T.-A., Mattern R.-H., Afargan M., Amitay O., Ziv O., Morgan B.A., Taylor J.E., Hoyer D., Goodman M. Design, synthesis, and biological activities of potent and selective somatostatin analogues incorporating novel peptoid residues. J Med Chem. 41:1998;2679-2685.
-
(1998)
J Med Chem
, vol.41
, pp. 2679-2685
-
-
Tran, T.-A.1
Mattern, R.-H.2
Afargan, M.3
Amitay, O.4
Ziv, O.5
Morgan, B.A.6
Taylor, J.E.7
Hoyer, D.8
Goodman, M.9
-
43
-
-
0033519190
-
Synthesis and biological evaluation of a cyclo-β-tetrapeptide as a somatostatin analogue
-
Gademann K., Ernst M., Hoyer D., Seebach D. Synthesis and biological evaluation of a cyclo-β-tetrapeptide as a somatostatin analogue. Angew Chem Int Ed Engl. 38:1999;1223-1226.
-
(1999)
Angew Chem Int Ed Engl
, vol.38
, pp. 1223-1226
-
-
Gademann, K.1
Ernst, M.2
Hoyer, D.3
Seebach, D.4
-
44
-
-
0035913057
-
Peptide folding induces high and selective affinity of a linear and small beta-peptide to the human somatostatin receptor 4
-
Gademann K., Kimmerlin T., Hoyer D., Seebach D. Peptide folding induces high and selective affinity of a linear and small beta-peptide to the human somatostatin receptor 4. J Med Chem. 44:2001;2460-2468.
-
(2001)
J Med Chem
, vol.44
, pp. 2460-2468
-
-
Gademann, K.1
Kimmerlin, T.2
Hoyer, D.3
Seebach, D.4
-
45
-
-
0033949970
-
The cyclo-β-tetrapeptide (β-HPhe-β-HThr-β-HLys-β-HTrp): Synthesis, NMR structure in methanol solution, and affinity for human somatostatin receptors
-
Gademann K., Ernst M., Seebach D., Hoyer D. The cyclo-β-tetrapeptide (β-HPhe-β-HThr-β-HLys-β-HTrp): synthesis, NMR structure in methanol solution, and affinity for human somatostatin receptors. Helv Chim Acta. 83:2000;16-33.
-
(2000)
Helv Chim Acta
, vol.83
, pp. 16-33
-
-
Gademann, K.1
Ernst, M.2
Seebach, D.3
Hoyer, D.4
-
46
-
-
0011928513
-
Biomimetic lung surfactant replacements
-
A.K. Dillow, & A. Lowman. New York: Marcel-Dekker Publishers
-
Wu C.W., Barron A.E. Biomimetic lung surfactant replacements. Dillow A.K., Lowman A. Biomimetic Materials and Design: Interactive Biointerfacial Strategies, Tissue Engineering, and Drug Delivery. 2002;565-633 Marcel-Dekker Publishers, New York.
-
(2002)
Biomimetic Materials and Design: Interactive Biointerfacial Strategies, Tissue Engineering, and Drug Delivery
, pp. 565-633
-
-
Wu, C.W.1
Barron, A.E.2
-
47
-
-
0002923074
-
A peptoid promise: Synthetic lung surfactant mimics may widen access to treatment of respiratory disease
-
Rouhi A.M. A peptoid promise: synthetic lung surfactant mimics may widen access to treatment of respiratory disease. Chem Eng News. 79:2001;50-51.
-
(2001)
Chem Eng News
, vol.79
, pp. 50-51
-
-
Rouhi, A.M.1
-
48
-
-
0032486757
-
Incorporation of achiral peptoid-based trimeric sequences into collagen mimetics
-
Jefferson E.A., Locardi E., Goodman M. Incorporation of achiral peptoid-based trimeric sequences into collagen mimetics. J Am Chem Soc. 120:1998;7420-7428.
-
(1998)
J Am Chem Soc
, vol.120
, pp. 7420-7428
-
-
Jefferson, E.A.1
Locardi, E.2
Goodman, M.3
-
49
-
-
0036007873
-
Insights on the conformational stability of collagen
-
Jenkins C.L., Raines R.T. Insights on the conformational stability of collagen. Nat Prod Rep. 19:2002;49-59.
-
(2002)
Nat Prod Rep
, vol.19
, pp. 49-59
-
-
Jenkins, C.L.1
Raines, R.T.2
-
50
-
-
0035969621
-
Toward β-peptide tertiary structure: Self-association of an amphiphilic 14-helix in aqueous solution
-
A 10-residue amphipathic 14-helix β-peptide was synthesized, and found to form either tetrameric or hexameric soluble aggregates in water solution, as assessed by analytical ultracentrifugation and NMR studies. Aggregate size was found to vary with buffer composition for unknown reasons. These results suggest the possibility of tertiary structure formation in a larger β-peptide oligomer that links several such helical motifs.
-
Raguse T.L., Lai J.R., LePlae P.R., Gellman S.H. Toward β-peptide tertiary structure: self-association of an amphiphilic 14-helix in aqueous solution. Org Lett. 3:2001;3963-3966. A 10-residue amphipathic 14-helix β-peptide was synthesized, and found to form either tetrameric or hexameric soluble aggregates in water solution, as assessed by analytical ultracentrifugation and NMR studies. Aggregate size was found to vary with buffer composition for unknown reasons. These results suggest the possibility of tertiary structure formation in a larger β-peptide oligomer that links several such helical motifs.
-
(2001)
Org Lett
, vol.3
, pp. 3963-3966
-
-
Raguse, T.L.1
Lai, J.R.2
LePlae, P.R.3
Gellman, S.H.4
-
51
-
-
0036015849
-
Toward the synthesis of artificial proteins: The discovery of an amphiphilic helical peptoid assembly
-
A combinatorial library of 15-residue amphipathic peptoids was synthesized, and screened for capacity to bind a fluorescent dye. Those peptoids with the best dye-binding performance were then analysed by size-exclusion chromatography, circular dichroism and analytical centrifugation. Results suggest the formation of water-soluble tetrameric peptoid aggregates, a potential harbinger of peptoid tertiary structure.
-
Burkoth T.S., Beausoleil E., Kaur S., Tang D., Cohen F.E., Zuckermann R.N. Toward the synthesis of artificial proteins: the discovery of an amphiphilic helical peptoid assembly. Chem Biol. 9:2002;647-654. A combinatorial library of 15-residue amphipathic peptoids was synthesized, and screened for capacity to bind a fluorescent dye. Those peptoids with the best dye-binding performance were then analysed by size-exclusion chromatography, circular dichroism and analytical centrifugation. Results suggest the formation of water-soluble tetrameric peptoid aggregates, a potential harbinger of peptoid tertiary structure.
-
(2002)
Chem Biol
, vol.9
, pp. 647-654
-
-
Burkoth, T.S.1
Beausoleil, E.2
Kaur, S.3
Tang, D.4
Cohen, F.E.5
Zuckermann, R.N.6
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