Search results for: Robert G. Stafford

Items from 1 to 8 out of 8 results

article

[¹⁸F]DPA-714 PET Imaging Reveals Global Neuroinflammation in Zika Virus-Infected Mice

Kyle Kuszpit, Bradley S. Hollidge, Xiankun Zeng, Robert G. Stafford, more

Molecular Imaging and Biology > 2018 > 20 > 2 > 275-283

Purpose The association of Zika virus (ZIKV) infection and development of neurological sequelae require a better understanding of the pathogenic mechanisms causing severe disease. The purpose of this study was to evaluate the ability and sensitivity of positron emission tomography (PET) imaging using [¹⁸F]DPA-714, a translocator protein (TSPO) 18 kDa radioligand, to detect and quantify neuroinflammation...

article

A Potent Peptidomimetic Inhibitor of Botulinum Neurotoxin Serotype A Has a Very Different Conformation than SNAP-25 Substrate

Jorge E. Zuniga, James J. Schmidt, Timothy Fenn, James C. Burnett, more

Structure > 2008 > 16 > 10 > 1588-1597

Botulinum neurotoxin serotype A is the most lethal of all known toxins. Here, we report the crystal structure, along with SAR data, of the zinc metalloprotease domain of BoNT/A bound to a potent peptidomimetic inhibitor (K _i = 41 nM) that resembles the local sequence of the SNAP-25 substrate. Surprisingly, the inhibitor adopts a helical conformation around the cleavage site, in contrast to...

article

Botulinum Neurotoxin Serotype F: Identification of Substrate Recognition Requirements and Development of Inhibitors with Low Nanomolar Affinity

James J. Schmidt, Robert G. Stafford

Biochemistry > 2005 > 44 > 10 > 4067 - 4073

article

Novel small molecule inhibitors of botulinum neurotoxin A metalloprotease activity

James C. Burnett, James J. Schmidt, Robert G. Stafford, Rekha G. Panchal, more

Biochemical and Biophysical Research Communications > 2003 > 310 > 1 > 84-93

Botulinum neurotoxins (BoNTs) are among the most lethal biological substances to have been weaponized and are listed as biodefense category A agents. Currently, no small molecule (non-peptidic) therapeutics exist to counter this threat; hence, identifying and developing compounds that inhibit BoNTs is a high priority. In the present study, a high-throughput assay was used to identify small molecules...

article

A high-affinity competitive inhibitor of type A botulinum neurotoxin protease activity

James J. Schmidt, Robert G. Stafford

FEBS Letters > 2002 > 532 > 3 > 423-426

The peptide N-acetyl-CRATKML-amide is an effective inhibitor of type A botulinum neurotoxin (BoNT A) protease activity [Schmidt et al., FEBS Lett. 435 (1998) 61-64]. To improve inhibitor binding, the peptide was modified by replacing cysteine with other sulfhydryl-containing compounds. Ten peptides were synthesized. One peptide adapted the structure of captopril to the binding requirements of BoNT...

article

High-Throughput Assays for Botulinum Neurotoxin Proteolytic Activity: Serotypes A, B, D, and F

James J. Schmidt, Robert G. Stafford, Charles B. Millard

Analytical Biochemistry > 2001 > 296 > 1 > 130-137

Botulinum neurotoxins (BoNT) are zinc metalloproteases that cleave and inactivate cellular proteins essential for neurotransmitter release. Because the paralytic effect of BoNT is a consequence of its enzymatic activity, selective inhibitors may be useful as drugs or as tools for further research. To expedite inhibitor discovery, we developed high-throughput, solid-phase protease activity assays for...

article

Type A botulinum neurotoxin proteolytic activity: development of competitive inhibitors and implications for substrate specificity at the S ₁ ' binding subsite

James J. Schmidt, Robert G. Stafford, Karen A. Bostian

FEBS Letters > 1998 > 435 > 1 > 61-64

Type A botulinum neurotoxin (botox A) is a zinc metalloprotease that cleaves only one peptide bond in the synaptosomal protein, SNAP-25. Single-residue changes in a 17-residue substrate peptide were used to develop the first specific, competitive inhibitors of its proteolytic activity. Substrate analog peptides with P ₄ , P ₃ , P ₂ ' or P ₃ ' cysteine were readily hydrolyzed...

article

Urinary elimination of saxitoxin after intravenous injection

Robert G. Stafford, Harry B. Hines

Toxicon > 1995 > 33 > 11 > 1501-1510

Paralytic shellfish poisoning is a serious public health concern throughout the world. An analytical method with diagnostic potential was used to isolate and measure saxitoxin, the most potent and studied paralytic shellfish poisoning toxin, in the urine of rats injected i.v. with sublethal doses (2 μg/kg) of saxitoxin. Urine was collected at intervals between 4 and 144 hr after injection. Saxitoxin...

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