Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:3.4.24.55 (
PTR
)
433
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Cyclo(PheN2-Tyr-D-Trp-Lys-Val-PheC3)-Thr-NH2 (
PTR
3046), a backbone-cyclic somatostatin analogue, was synthesized by solid-phase methodology. The binding characteristics of
PTR
3046 to the different somatostatin receptors, expressed in CHO cells, indicate high selectivity to the SSTR5 receptor.
PTR
3046 is highly stable against enzymatic degradation as determined in vitro by incubation with rat renal homogenate and human serum. The biological activity of
PTR
3046 in vivo was determined in rats.
PTR
3046 inhibits bombesin- and caerulein-induced amylase and lipase release from the pancreas without inhibiting growth hormone or glucagon release. The major conformation of
PTR
3046 in CD3OH, as determined by
NMR
, is defined by a type II' beta-turn at D-Trp-Lys and a cis amide bond at Val-PheC3.
...
PMID:A backbone-cyclic, receptor 5-selective somatostatin analogue: synthesis, bioactivity, and nuclear magnetic resonance conformational analysis. 952 66
A backbone bridged and disulfide bridged bicyclic somatostatin analogue, compound 1 (
PTR
-3205), was designed and synthesized by solid-phase methodology. The binding of compound 1 to the five different somatostatin receptors, expressed in CHO or COS-7 cells, indicate a high degree of selectivity towards hsstr2. The three-dimensional structure of this compound has been determined in DMSO-d(6) and in water by 1H
NMR
and by molecular dynamics simulations. Similar backbone conformations were observed in both solvents. We have established direct evidence that the backbone of this bicyclic somatostatin analogue assumes a 'folded' conformation in solution, where the lactam ring extends roughly in the plane of the beta-turn. The pharmacophoric region Phe-(D)-Trp-Lys-Thr of compound 1 is in accord with that of both the Veber compound L-363,301 (Merck) and sandostatin. We believe that the enhanced selectivity towards the hsst2 receptor, in comparison with other analogues, is due to its large hydrophobic region, composed of the lactam ring and the Phe side chains at positions 1 and 8.
...
PMID:A bicyclic and hsst2 selective somatostatin analogue: design, synthesis, conformational analysis and binding. 1171 1
Zinc modulates the biological function of histidine-rich glycoprotein (HRG) through binding to its His-rich region (HRR). The Zn
2+
-binding properties of a 35 amino-acid biologically-active peptide mimic of the HRR, HRGP330, were investigated using dissociative mass spectrometry approaches in addition to travelling-wave ion mobility mass spectrometry (TWIM-MS). Native mass spectrometry confirmed zinc binding to HRGP330; however, broadening of the
1
H
NMR
resonances upon addition of Zn
2+
ions precluded the attainment of structural information. A complementary approach employing TWIM-MS indicated that HRGP330 has a more compact structure in the presence of Zn
2+
ions. Top-down MS/MS data supported a metal-binding-induced conformational change, as fewer fragments were observed for Zn
2+
-bound HRGP330. Zn
2+
-bound fragments of both N-terminal and C-terminal ends of the peptide were identified from collision-induced dissociation (CID) and electron transfer dissociation/proton transfer reaction (ETD/
PTR
) experiments, suggesting that multiple binding sites exist within this region of HRG. The combination of mass spectrometry and
NMR
approaches provides new insight into the highly dynamic interaction between zinc and this His-rich peptide.
...
PMID:Native electrospray mass spectrometry approaches to probe the interaction between zinc and an anti-angiogenic peptide from histidine-rich glycoprotein. 2987 14
