Peptidomimetics—Tailored Enzyme Inhibitors

Wiley - Tập 33 Số 17 - Trang 1699-1720 - 1994
Joachim Gante1
1Präklinische Pharmaforschung, Medizinische Chemie, D‐64271 Darmstadt (FRG), Telefax: Int. code (6151)72‐2000

Tóm tắt

AbstractPeptides and proteins (there is no clear boundary between the two classes of compounds) are absolutely essential components of organisms in many ways. While proteins have biocatalytic functions and are important components of tissues, peptides play an important role in the organism as hormones, neurotransmitters, and neuromodulators. Peptides and their analogues have long been used in medicinal chemistry as therapeutic agents for pathological conditions generally characterized by a disruption of the interplay between messenger molecules or enzyme substrates and their targets, the receptors and enzymes. For various biochemical and biophysical reasons there is an increasing tendency towards the use of chemical “Trojan horses” known as peptidomimetics. The chances that such agents are active generally increase with the magnitude of the “deceptive effect”, in other words in proportion to the degree of conversion of a peptide into a non‐peptide. Rational design has become a catchphrase which is at present applied frequently to the development of peptidomimetics. New computer programs are invaluable tools in such design processes. However, in spite of the many advances already made, we are still far from the final goal, the de novo design of peptidomimetics. Rational design is nonetheless advancing rapidly, and it is already clear that developments in the area of peptidomimetics have given a great boost to peptide chemistry as a whole. This can be expected to continue, so that in future peptide chemistry may be characterized by a type of symbiotic alliance between peptides and non‐peptides.

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Tài liệu tham khảo

A peptidomimetic is defined as a substance having a secondary structure as well as other structural features analogous to that of the original peptide which allows it to displace the original peptide from receptors or enzymes. As a result the effects of the original peptide are inhibited (antagonist inhibitor) or duplicated (agonist).

10.1002/recl.19941130102

10.1002/ange.19931050905

10.1002/anie.199312441

10.1002/med.2610130305

10.1021/jm00073a001

Spatola A. F., 1993, Methods in Neurosciences, Vol. 13, 19

Morgan B. A., 1989, Annu. Rep. Med. Chem., 24, 244

Spatola A. F., 1983, Chemistry and Biochemistry of Amino Acids, Peptides, and Proteins, Vol. VII, 267

10.1002/bip.360330709

1994, Nachr. Chem. Tech. Lab., 42, 164

(j)M.Kahn Synlett1993 821;

10.1002/recl.19941130202

10.1002/ange.19921040404

10.1002/anie.199203673

Radunz H. E., 1992, GIT Fachz. Lab., 36, 869

10.1016/S0040-4020(01)90211-X

10.1016/0223-5234(90)90113-H

10.1002/ardp.19913240705

(c)M.Mittakanti D. A.Feakes K. W.Morse Synthesis1992 380.

10.1016/S0040-4020(01)86293-1

(b)D.Merricks P. G.Sammes E. R.Walker K.Henrick M. M.McPartlin J. Chem. Soc. Perkin Trans. 11991 2169;

10.1016/S0040-4039(00)92641-8

1992, Tetrahedron Lett., 33, 3689

10.1016/S0960-894X(01)81171-9

10.1016/S0040-4020(01)92278-1

10.1016/S0021-9258(17)44751-X

10.1021/jm00150a027

10.1016/S0021-9258(17)42521-X

10.1016/S0040-4020(01)86110-X

10.1016/S0040-4020(01)80252-0

10.1016/S0040-4020(01)86125-1

10.1021/jo00233a006

Manesis N., 1986, Biopolymers, 25, 97

10.1021/ja00002a067

J.Di Maio B.Bellau J. Chem. Soc. Perkin Trans. 11989 1687.

10.1126/science.7001627

10.1021/jo00340a023

10.1135/cccc19840642

10.1021/jo00219a041

10.1021/jo00259a003

10.1021/jm00402a021

10.1021/jm00117a022

10.1021/jo00274a037

(i)G.Valle M.Crisma C.Toniolo K.‐L.Yu R. L.Johnson J. Chem. Soc. Perkin Trans. 21989 83;

10.1021/jo00290a026

10.1016/S0040-4039(00)80047-7

10.1016/S0960-894X(01)80882-9

10.1016/S0040-4039(00)82132-2

J.Zabrocki G. D.Smith J. B.Dunbar Jr. K. W.Marshall M.Toth G. R.Marshall Pept. Proc. Eur. Pept. Symp. 20th 19881989 295.

10.1016/S0960-894X(00)80692-7

Jones R., 1988, Tetrahedron Lett., 29, 3858

10.1021/jm00086a017

10.1016/S0040-4039(00)79701-2

10.1016/S0040-4020(01)90205-4

10.1016/S0040-4020(01)90207-8

G.Hölzemann Kontakte (Darmstadt)1991(1) 3;

Kontakte (Darmstadt)1991(2) 55;

Bailey P. D., 1990, Peptide Chemistry, 182

10.1021/ja00261a033

10.1016/S0040-4020(01)80237-4

10.1002/hlca.19940770110

(a)K.Sato U.Nagai J. Chem. Soc. Perkin Trans. 119861231;

10.1016/S0040-4020(01)90216-9

10.1016/S0040-4039(00)80678-4

10.1021/ja00049a005

10.1016/S0040-4020(01)90217-0

10.1021/jm00099a027

10.1016/S0040-4020(01)90208-X

10.1016/0006-291X(92)91296-3

M.Kahn M.Lee H.Nakanishi J.Urban B.Gardner Proc. Am. Pept. Symp. 13th 1993 in press;

Müller K., 1993, Perspectives in Medicinal Chemistry, 513

10.1021/jo00023a037

10.1021/jo00023a038

10.1016/S0040-4020(01)90219-4

C. A.Dinarello Adv. Immunol.1989 153.

10.1021/bi00717a024

Rich D. H., 1993, Med. Res. Rev., 13, 368

Tanford C., 1980, The Hydrophobic Effect: Formation of Micelles and Biological Membranes

10.1021/jm00101a017

10.1021/ja00050a082

10.1016/S0040-4020(01)90222-4

10.1021/ja00079a039

10.1021/ja00049a081

10.1016/S0040-4020(01)90214-5

10.1002/ange.19911031008

10.1002/anie.199112781

10.1007/978-94-011-2264-1_1

10.1073/pnas.83.13.4918

10.1021/jm00129a003

10.1021/jm00099a020

10.1021/jm00077a002

10.1021/jm00167a007

10.1021/jm00108a043

J. M.Samenen C. E.Peishoff R. M.Keenan J.Weinstock Bioorg. Med. Chem. Lett.1993 909.

10.1021/jm00031a004

10.1021/jm00186a020

10.1021/jm00397a026

10.1021/jm00398a012

10.1002/nadc.19900380409

10.1021/jm00126a039

10.1021/jm00117a027

10.1073/pnas.86.24.9752

10.7164/antibiotics.36.1787

10.1271/bbb1961.48.1661

10.7164/antibiotics.39.734

10.1021/jo00223a037

10.1021/jo00375a014

10.1016/S0040-4039(00)85983-3

B.Lygo Synlett1992 793.

J.Gante U.Anlauf R.Weitzel Pept. Proc. Eur. Pept. Symp. 21st 19921993 605.

10.1021/jm00096a004

10.1016/0014-5793(91)80441-5

10.1016/S0040-4039(01)91316-4

(b)Y. A.Fehrentz B.Castro Synthesis1983 676.

10.1021/jo00332a045

Guichard G., 1993, Pept. Res., 6, 121

(a) Review:J.Gante Synthesis1989405;

(b)A. S.Dutta J. S.Morley J. Chem. Soc. Perkin Trans. 11975 1712.

10.1002/cber.19650981034

J.Gante M.Krug G.Lauterbach R.Weitzel Proc. Am. Pept. Symp. 13th 1993 1994 299.

10.1021/jm00101a004

10.1021/jm00115a016

J.Gante H.Kahlenberg Liehigs Ann. Chem.1989 1085.

J.Gante R.Weitzel Liebigs Ann. Chem.1990 349.

Gante J., 1991, Chem. Ztg., 115, 215

C. J.Gray M.Quibell K. L.Jiang N.Bagett Innovation Perspect. Solid Phase Synth. Collect. Pap. Int. Symp. 2nd 19911992 295.

10.1016/0040-4020(77)80185-3

10.1016/S0960-894X(00)80516-8

10.1002/ange.19921041025

10.1002/anie.199213911

10.1021/ja00042a052

10.1021/ja00042a053

10.1021/jo00073a010

10.1073/pnas.90.17.8048

10.1021/ja00052a093

10.1073/pnas.89.20.9367

10.1021/ja00052a076

1993, Chemtracts: Macromol. Chem., 4, 80

10.1002/ange.19931050408

10.1002/anie.199305431

10.1021/ar00029a007

10.1016/S0040-4039(00)96384-6

10.1016/S0065-3233(08)60402-7

Page M. I., 1990, Compr. Med. Chem., 2, 61

Rich D. H., 1990, Compr. Med. Chem., 2, 391

Collective term for enzymes that catalyze the hydrolytic cleavage of the peptide bond in proteins and peptides:Römpp Chemie‐Lexikon Thieme Stuttgart 1992 p. 3647.

Barrett A. J., 1986, Proteinase‐Inhibitors, Res. Monogr. Cell Tissue Physiol., 13, 301

Banner D., 1993, Perspectives of Medicinal Chemistry, 27

10.1146/annurev.bi.46.070177.001555

Rich D. H., 1986, Res. Monogr. Cell Tissue Physiol., 12, 153

Rich D. H., 1986, Res. Monogr. Cell Tissue Physiol., 12, 179

10.1073/pnas.84.20.7009

Hofmann T., 1984, Biochemistry, 23, 5253

10.1002/med.2610130605

10.1021/bi00319a011

10.1016/S0006-291X(67)80055-X

10.1016/0006-291X(68)90326-4

Rich D. H., 1990, Compr. Med. Chem., 2, 414

Rich D. H., 1990, Compr. Med. Chem., 2, 400

10.1073/pnas.77.9.5476

10.1016/S0006-291X(80)80158-6

10.1021/jm00030a008

(a)M.Szelke D. M.Jones B.Atrash A.Hallett B. J.Leckie Pept. Struct. Funct. Proc. Am. Pept. Symp. 8th 1983 1983 579;

10.1042/bst0120948

10.1042/bst0120956

10.7164/antibiotics.23.259

10.1146/annurev.mi.36.100182.000451

10.1093/ajh/2.11.819

Clozel J.‐P., 1993, Arzneim. Forsch., 43, 260

Ogihara T., 1992, Hypertension, 20

10.1021/jm00092a006

10.1021/jm00088a005

10.1097/00005344-199301000-00022

10.1021/bi00815a005

10.1021/bi00798a004

10.1016/S0021-9258(19)45746-3

10.1021/bi00735a008

10.1126/science.191908

10.1002/med.2610050405

10.1038/288280a0

10.3109/10409238409108720

10.1002/9780470123034.ch1

10.1016/0014-5793(82)81036-3

(b)C. H.Hassall A.Krohn C. J.Moody W. A.Thomas J. Chem. Soc. Perkin Trans. 11984 155.

10.1021/jm00058a006

Rich D. H., 1990, Compr. Med. Chem., 2, 400

10.1002/med.2610050405

10.1111/j.1476-5381.1990.tb12056.x

10.7164/antibiotics.40.468

Shirota M., 1992, Arzneim. Forsch., 42, 1430

10.1021/jm00100a024

Wiley R. A., 1993, Med. Chem. Rev., 13, 350

10.1055/s-2007-1002418

10.1016/S0065-7743(08)60409-1

10.1111/j.1749-6632.1981.tb29757.x

10.1016/0005-2744(79)90103-7

10.1055/s-2007-1002418

Mustard J. F., 1970, Phamacol. Rev., 22, 97

10.1083/jcb.77.3.774

Jaques L. B., 1980, Pharmacol. Rev., 31, 99

10.1055/s-2007-1003530

Markwardt F., 1985, Biomed. Biochim. Acta, 44, 1007

10.1021/bi00482a021

10.1021/bi00241a004

10.1021/bi00364a025

10.1055/s-2007-1002722

Talbot M. D., 1990, Drugs News Perspect., 3, 357

10.1111/j.1749-6632.1981.tb29786.x

10.1073/pnas.85.9.3184

10.1021/jm00168a030

Kaiser B., 1991, Pharmazie, 46, 128

10.1002/j.1460-2075.1989.tb08511.x

10.1016/S0021-9258(17)44751-X

10.1021/bi00420a018

10.1021/bi00445a015

10.1021/jm00065a005

Knabb R. M., 1992, Thromb. Haemostasis, 67, 56, 10.1055/s-0038-1648379

10.1016/0006-291X(81)91279-1

10.1021/bi00296a014

10.1161/01.CIR.82.4.1476

Mellott M. J., 1990, Thromb. Haemostasis, 64, 526, 10.1055/s-0038-1647352

10.1016/0049-3848(83)90218-9

10.1016/S0021-9258(18)54894-8

W.Stüber(Behringwerke AG) EP‐B 508220 1992.

W.Stüber unpublished see also ref. [128].

10.1021/jm00055a002

10.1021/bi00482a021

10.1016/S0021-9258(18)45796-1

10.1021/jm00096a004

10.1021/jm00096a010

Owen T. J., 1988, J. Chem. Chem., 31, 1009

10.1111/j.1432-1033.1990.tb19320.x

10.1038/332411a0

Opgenoth T. J., 1992, FASEB J., 6, 2653, 10.1096/fasebj.6.9.1612289

10.1021/jm00087a001

10.1161/01.HYP.15.6.729

10.1016/0014-2999(90)90346-8

10.1016/0024-3205(90)90392-5

10.1016/0024-3205(91)90249-B

10.1016/0006-291X(89)92258-4

10.1073/pnas.88.3.703

10.1016/0006-291X(90)90685-G

10.1016/0024-3205(93)90697-2

10.1093/ajh/6.8.667

10.1021/jm00053a023

10.1042/bst0210697

10.1016/0006-291X(90)92104-8

10.1016/0006-291X(90)92014-Q

10.1016/0006-291X(90)90758-F

10.1016/0014-5793(90)81060-2

10.1021/jm00056a007

10.1073/pnas.83.6.1911

10.1038/325773a0

10.1146/annurev.bi.62.070193.002551

10.1007/BF02171658

10.1021/jm00112a001

10.3109/14756369209041357

Williams R. M., 1993, Biomed. Appl. Biotechnol., 1, 204

Grant S. K., 1993, Biomed. Appl. Biotechnol., 1, 349

10.1126/science.2420008

10.1073/pnas.85.13.4686

10.1021/jm00113a025

10.1021/jm00107a049

10.1126/science.2183354

10.1021/jm00172a002

10.1126/science.2548279

10.1038/337615a0

10.1016/S0960-894X(01)81222-1

10.1021/ja00024a061

10.1016/0006-291X(90)92010-W

10.1002/ange.19931051245

10.1002/anie.199317201

10.1021/bi00082a019

10.1021/jm00099a008

10.1016/S0040-4039(00)60317-9

10.1021/jm00059a019

10.1021/ja00055a069

10.1021/jm00054a015

H. L.Sham D. A.Betebenner C.Zhao N. E.Wideburg A.Saldivar D. J.Kempf J. J.Plattner D. W.Norbeck J. Chem. Soc. Chem. Cutmmun.1993 1052.

10.1016/S0960-894X(00)80673-3

10.1021/jm00060a001

Roques B. P., 1986, NIDA Res. Monogr., 70, 128

10.1161/01.HYP.7.4.469

10.1093/ajh/4.10.850

Ruskoako H., 1992, Pharmcol. Rev., 44, 479

10.1016/S0140-6736(89)90714-9

10.1097/00004872-199203000-00011

10.1038/288286a0

10.1016/0006-291X(80)91371-6

Sybertz E. J., 1989, J. Pharmacol. Exp. Ther., 250, 624

10.1021/jm00053a011

10.1016/0196-9781(92)90053-6

10.1111/j.1476-5381.1992.tb14312.x

10.1016/S0960-894X(00)80674-5

10.1002/med.2610140202

10.1021/bi00384a005

Woessner J. F., 1980, Collagenases in Normal and Pathological Tissue, 223

10.1021/jm00077a006

10.1021/jm00027a020

10.1038/337476a0

10.1016/S0021-9258(19)67841-5

10.1002/ange.19941061404

10.1002/anie.199414151

10.1016/S0040-4039(00)79671-7

10.1126/science.1700475

10.1021/ja00056a067

10.1016/0968-0004(83)90165-2

Barrett A. J., 1980, Mammalian Proteinases: A Glossary and Bibliography, Vol. 1.

10.1021/jm00062a009

10.1126/science.8316834

10.1021/jm00032a004

10.1126/science.8316833

Garcia A. M., 1993, J. Biol. Chem., 268, 18415, 10.1016/S0021-9258(17)46638-5

10.1002/j.1460-2075.1984.tb02177.x

10.1016/0092-8674(89)90054-8

Gibbs J. B., 1993, J. Biol. Chem., 268, 7617, 10.1016/S0021-9258(18)52998-7

10.1021/bi00130a010

Goldstein J. L., 1991, J. Biol. Chem., 266, 15575, 10.1016/S0021-9258(18)98441-3

10.1073/pnas.89.17.8313

Rich D. H., 1993, Perspectives in Medicinal Chemistry, 15

Tanford C., 1980, The Hydrophobic Effect: Formation of Micelles and Biological Membranes

10.1021/ja00033a048

10.1126/science.1566062

10.1002/prot.340110409

Bartlett P. A., 1989, Molecular Recognition: Chemical and Biochemical Problems, 182

10.1016/S0040-4020(01)90221-2

(a)Addendum: Many publications on the topics in this review have appeared since the submission of this manuscript. A selection (up to April 1994) are listed here. Structure:M.Quibell W. G.Turnell T.Johnson J. Chem. Soc. Perkin Trans. 119932843;

10.1016/S0040-4039(00)76227-7

10.1016/S0040-4039(00)76226-5

10.1002/ange.19941060615

10.1002/anie.199406871

10.1021/ja00085a014

10.1021/ja00081a063

10.1002/med.2610140104

10.1111/j.1399-3011.1994.tb00388.x

10.1002/bip.360330715

10.1021/jm00076a010

10.1021/jm00068a022

Patel A., 1993, Prog. Med. Chem., 30, 328

10.1021/jm00030a009

10.1016/S0960-894X(01)80150-5

French J., 1994, J. Pharmacol. Exp. Ther., 268, 180

10.1021/jm00034a005

10.1002/med.2610130605

10.1039/c39930001052

10.1016/S0960-894X(01)81216-6

10.1021/jm00069a018

10.1021/jm00073a012

10.1021/jm00073a010

10.1016/S0960-894X(00)80308-X

10.1021/jm00068a008

Sham H. L., 1993, FEBS Lett., 329

10.1021/jm00068a006

10.1002/bdd.2510140806

10.1021/jo00069a024

10.1016/S0040-4020(01)81896-2

10.1021/jm00073a011

10.1021/jm00028a001

10.1016/S0960-894X(01)80186-4

10.1016/S0960-894X(01)80159-1

10.1016/0960-894X(94)80025-1

10.1021/ja00082a004

10.1002/ange.19941060630

10.1002/anie.199406851

10.1021/jm00028a001

Okamoto S., 1993, Methods Enzymol., 222, 238

10.1016/0076-6879(93)23053-P

10.1016/0165-6147(93)90095-2

10.1021/jm00031a012

10.1021/jm00028a004

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Wiley

Tập 33 Số 17

1699-1720

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