Page last updated: 2024-12-06

85548e

Description Research Excerpts Clinical Trials Roles Classes Pathways Study Profile Bioassays Related Drugs Related Conditions Protein Interactions Research Growth

Description

85548e: structure given in first source; RN given for (2S-(2R*,4R*,5R*))-isomer [Medical Subject Headings (MeSH), National Library of Medicine, extracted Dec-2023]

Cross-References

ID Source	ID
PubMed CID	449613
CHEMBL ID	2062130
MeSH ID	M0200907

Synonyms (8)

Synonym
(2s)-2-[[(2s,3s)-2-[[(2s,4s,5s)-5-[[(2s)-4-amino-2-[[(2s)-5-amino-2-[[(2s)-2-[[(2s)-2-amino-3-methyl-butanoyl]amino]-3-hydroxy-propanoyl]amino]-5-oxo-pentanoyl]amino]-4-oxo-butanoyl]amino]-4-hydroxy-2-isopropyl-7-methyl-octanoyl]amino]-3-methyl-pentanoyl]
u-85548e
h-val-ser-gln-asn-leu-.psi.[ch(oh)ch2]-val-ile-val-oh
8HVP
CHEMBL2062130 ,
85548e
bdbm50230843
AKOS040746491

[information is derived through text-mining from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Protein Targets (3)

Inhibition Measurements

Protein	Taxonomy	Measurement	Average	Min (ref.)	Avg (ref.)	Max (ref.)	Bioassay(s)
Chain A, HIV-1 PROTEASE	Human immunodeficiency virus 1	Ki	0.0010	0.0010	0.0010	0.0010	AID977610
Chain B, HIV-1 PROTEASE	Human immunodeficiency virus 1	Ki	0.0010	0.0010	0.0010	0.0010	AID977610
Protease	Human immunodeficiency virus 1	Ki	0.0010	0.0000	0.0443	3.1000	AID162713
[prepared from compound, protein, and bioassay information from National Library of Medicine (NLM), extracted Dec-2023]

Bioassays (3)

Assay ID	Title	Year	Journal	Article
AID977610	Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB	1991	Biochemistry, Feb-12, Volume: 30, Issue:6	Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
AID1811	Experimentally measured binding affinity data derived from PDB	1991	Biochemistry, Feb-12, Volume: 30, Issue:6	Structure at 2.5-A resolution of chemically synthesized human immunodeficiency virus type 1 protease complexed with a hydroxyethylene-based inhibitor.
AID162713	Binding affinity against HIV-1 aspartic proteinase was determined	1993	Journal of medicinal chemistry, Jul-23, Volume: 36, Issue:15	Multiple copy simultaneous search and construction of ligands in binding sites: application to inhibitors of HIV-1 aspartic proteinase.
[information is prepared from bioassay data collected from National Library of Medicine (NLM), extracted Dec-2023]

Research

Studies (6)

Timeframe	Studies, This Drug (%)	All Drugs %
pre-1990	0 (0.00)	18.7374
1990's	5 (83.33)	18.2507
2000's	1 (16.67)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Study Types

Publication Type	This drug (%)	All Drugs (%)
Trials	0 (0.00%)	5.53%
Reviews	0 (0.00%)	6.00%
Case Studies	0 (0.00%)	4.05%
Observational	0 (0.00%)	0.25%
Other	7 (100.00%)	84.16%
[information is prepared from research data collected from National Library of Medicine (NLM), extracted Dec-2023]

Substance	Relationship Strength	Studies	Classes	Roles
aspartic acid Aspartic Acid: One of the non-essential amino acids commonly occurring in the L-form. It is found in animals and plants, especially in sugar cane and sugar beets. It may be a neurotransmitter.. aspartic acid : An alpha-amino acid that consists of succinic acid bearing a single alpha-amino substituent. L-aspartic acid : The L-enantiomer of aspartic acid.	1.98	1	aspartate family amino acid; aspartic acid; L-alpha-amino acid; proteinogenic amino acid	Escherichia coli metabolite; mouse metabolite; neurotransmitter
n-acetylseryl-leucyl-asparaginyl(phenylalanyl-hydroxyethylamino-prolyl)isoleucyl-valyl methyl ester N-acetylseryl-leucyl-asparaginyl(phenylalanyl-hydroxyethylamino-prolyl)isoleucyl-valyl methyl ester: inhibitor of HIV Protease; structure given in first source; RN given is for (S-(R,R)) isomer	1.98	1
jg 365 [no description available]	2.38	2
mvt 101 [no description available]	1.98	1
u 75875 U 75875: structure given in first source	1.99	1
streptomyces pepsin inhibitor [no description available]	1.98	1
mvt 101 MVT 101: peptide inhibitor	1.97	1

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