Lysyl 4-aminobenzoic acid derivatives as potent small molecule mimetics of plasminogen kringle 5

George S. Sheppard; Megumi Kawai; Richard A. Craig; Donald J. Davidson; Sandra M. Majest; Randy L. Bell; Jack Henkin

doi:10.1016/j.bmcl.2003.12.034

Lysyl 4-aminobenzoic acid derivatives as potent small molecule mimetics of plasminogen kringle 5

George S. Sheppard^*, Megumi Kawai, Richard A. Craig, Donald J. Davidson, Sandra M. Majest, Randy L. Bell, Jack Henkin

^*Corresponding author for this work

CLP - Chemistry of Life Processes Institute

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Kringle 5, a proteolytic fragment of human plasminogen has been shown to potently inhibit angiogenesis. The tetrapeptide KLYD derived from kringle 5 has been shown to capture many activities of kringle 5 in vitro. Further simplification has been achieved by replacement of the two central amino acids with a 4-aminobenzoic acid spacer group. Molecules displaying the required recognition groups on this core show similar in vitro properties to kringle 5, and are able to displace radiolabeled protein from a high affinity binding site on endothelial cells.

Original language	English (US)
Pages (from-to)	965-966
Number of pages	2
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	14
Issue number	4
DOIs	https://doi.org/10.1016/j.bmcl.2003.12.034
State	Published - Feb 23 2004

ASJC Scopus subject areas

Drug Discovery
Molecular Medicine
Molecular Biology
Biochemistry
Clinical Biochemistry
Pharmaceutical Science
Organic Chemistry

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abstract = "Kringle 5, a proteolytic fragment of human plasminogen has been shown to potently inhibit angiogenesis. The tetrapeptide KLYD derived from kringle 5 has been shown to capture many activities of kringle 5 in vitro. Further simplification has been achieved by replacement of the two central amino acids with a 4-aminobenzoic acid spacer group. Molecules displaying the required recognition groups on this core show similar in vitro properties to kringle 5, and are able to displace radiolabeled protein from a high affinity binding site on endothelial cells.",

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AU - Sheppard, George S.

AU - Kawai, Megumi

AU - Craig, Richard A.

AU - Davidson, Donald J.

AU - Majest, Sandra M.

AU - Bell, Randy L.

AU - Henkin, Jack

PY - 2004/2/23

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AB - Kringle 5, a proteolytic fragment of human plasminogen has been shown to potently inhibit angiogenesis. The tetrapeptide KLYD derived from kringle 5 has been shown to capture many activities of kringle 5 in vitro. Further simplification has been achieved by replacement of the two central amino acids with a 4-aminobenzoic acid spacer group. Molecules displaying the required recognition groups on this core show similar in vitro properties to kringle 5, and are able to displace radiolabeled protein from a high affinity binding site on endothelial cells.

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Lysyl 4-aminobenzoic acid derivatives as potent small molecule mimetics of plasminogen kringle 5

Abstract

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