# BIOCHEMISTRY:  MECHANISM OF ACTION OF PENICILLIN

> **NIH NIH R01** · HARVARD UNIVERSITY · 1989 · $84,761

## Abstract

The general objective of the present work is to study in as much detail as
possible the mechanism of inhibition of bacterial growth by penicillins,
cephalosporins and other Beta-lactam antibodies.  During the present phase
the main effort will be:

1) to elucidate the sequences of the active site peptides of the high
molecular weight penicillin binding proteins of Escherichia coli (PBPs 1a,
1b, 2 and 3) in order to localize the active site peptides within the
primary amino acid sequences derived from DNA clones,

2) similarly, to identify and localize the hydrophobic membrane-spanning
peptide(s) of these penicillin-binding proteins as well as that of PBP 5 and

3) to crystallize one or more of these penicillin-binding proteins, either
in the presence of the detergent or as a catalytically active water soluble
proteolytic degradation product, in order to determine the x-ray
crystallographic structure.

These data should provide much useful information for the improved rational
design of penicillins, cephalosporins and related Beta-lactam antibiotics.

## Key facts

- **NIH application ID:** 3124513
- **Project number:** 5R01AI009152-21
- **Recipient organization:** HARVARD UNIVERSITY
- **SAM.gov UEI:** LN53LCFJFL45
- **Principal Investigator:** JACK L STROMINGER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1989
- **Award amount:** $84,761
- **Award type:** 5
- **Project period:** 1975-01-01 → 1990-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3124513

## Citation

> US National Institutes of Health, RePORTER application 3124513, BIOCHEMISTRY:  MECHANISM OF ACTION OF PENICILLIN (5R01AI009152-21). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3124513. Licensed CC0.

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