EurekaMag
+ Translate
+ Most Popular
Advantages and disadvantages of bordeaux mixture and of lime-sulphur used on apples in the growing season
Observations on the Umaria marine bed
10 years of hearing conservation in the Royal Air Force
Chocolate crumb - dairy ingredient for milk chocolate
Effect of daily gelatin ingestion on human scalp hair
Comparison of rice bran and maize bran as feeds for growing and fattening pigs
The composition of pampas-grass (Cortaderia argentea.)
The Accraian Series:
The mechanism of the Liebermann-Burchard reaction of sterols and triterpenes and their esters
Cerebrovascular Doppler ultrasound studies (cv-Doppler)
Toria: PT-303 - first national variety
Hair growth promoting activity of tridax procumbens
Productivity of Pekin x Khaki Campbell ducks
A stable cytosolic expression of VH antibody fragment directed against PVY NIa protein in transgenic potato plant confers partial protection against the virus
Solar treatment of wheat loose smut
Swimmers itch in the Lake of Garda
Bactofugation and the Bactotherm process
The effects of prefrontal lobotomy on aggressive behavior in dogs
Visual rating scales for screening whorl-stage corn for resistance to fall armyworm
Breakdown of seamounts at the trench axis, viewed from gravity anomaly
Kooken; pennsylvania's toughest cave
Recovery of new dinosaur and other fossils from the Early Cretaceous Arundel Clay facies (Potomac Group) of central Maryland, U.S.A
Zubor horny (Bison bonasus) v prirodnych podmienkach Slovensku
The extended Widal test in the diagnosis of fevers due to Salmonella infection
Hair of the american mastodon indicates an adaptation to a semi aquatic habitat

Role of peptide structure in lipid-peptide interactions: high-sensitivity differential scanning calorimetry and electron spin resonance studies of the structural properties of dimyristoylphosphatidylcholine membranes interacting with pentagastrin-related pentapeptides


Role of peptide structure in lipid-peptide interactions: high-sensitivity differential scanning calorimetry and electron spin resonance studies of the structural properties of dimyristoylphosphatidylcholine membranes interacting with pentagastrin-related pentapeptides



Biochemistry 24(13): 3135-3144



ISSN/ISBN: 0006-2960

PMID: 2992577

DOI: 10.1021/bi00334a010

The effects of amino acid substitutions in the pentapeptide pentagastrin on the nature of its interactions with dimyristoylphosphatidylcholine (DMPC) are assessed by differential scanning calorimetry and electron spin resonance. In two peptide analogues, the Asp at position 4 in pentagastrin (N-t-Boc-beta-Ala-Trp-Met-Asp-Phe-NH2) is replaced by Gly or Phe. These uncharged, more hydrophobic peptides have little effect on the transition temperature of DMPC, but they broaden the transition and lower the transition enthalpy as do integral membrane proteins. These peptides also mimic the behavior of integral membrane proteins in decreasing the order of a 5-doxylstearic acid spin probe below the transition temperature and in exhibiting a second immobilized lipid component using a 16-doxylstearic acid spin probe in DMPC. Three charged peptides were studied: pentagastrin, an analogue with positions 4 and 5 reversed (i.e., ending in Phe-Asp-NH2), and one with Asp replaced by Arg at position 4. All three of these charged peptides altered the phase transition behavior of DMPC to give two components, one above and one below the transition temperature of the pure lipid. With increasing peptide concentration, the higher melting transition became more prominent. The arginine-containing peptide produced the largest shifts in melting temperature followed by pentagastrin and then the "reversed" peptide. The arginine-containing peptide also increased the enthalpy of the transition. These peptides also increased the ordering of DMPC below the phase transition as measured with both 5- and 16-doxylstearic acid. The ordering effect was most pronounced with the arginine-containing peptide using the 5-doxylstearic acid probe. The results demonstrate that even the zwitterionic DMPC can interact more strongly with positively charged peptides than with negatively charged ones. In addition, peptide sequence as well as composition is important in determining the nature of peptide-lipid interactions. The markedly different effects of these pentagastrin peptides on the phase transition and motional properties of DMPC occur despite the similar depth of burial of these peptides with DMPC.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 018102489

Download citation: RISBibTeXText

Related references

Role of peptide structure in lipid-peptide interactions: nuclear magnetic resonance study of the interaction of pentagastrin and [Arg4]pentagastrin with dimyristoylphosphatidylcholine. Chemistry and Physics of Lipids 49(1-2): 105-110, 1988

Role of peptide structure in lipid-peptide interactions: a fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles. Biochemistry 23(25): 6072-6077, 1984

Role of peptide structure in lipid peptide interactions nmr study of the interaction of pentagastrin and 4 arginine pentagastrin with dimyristoylphosphatidylcholine. Chemistry and Physics of Lipids 49(1-2): 105-110, 1988

Interactions of angiotensin II non-peptide AT(1) antagonist losartan with phospholipid membranes studied by combined use of differential scanning calorimetry and electron spin resonance spectroscopy. Biochimica et Biophysica Acta 1461(1): 135-146, 1999

Differential scanning calorimetry and Fourier transform infrared spectroscopic studies of phospholipid organization and lipid-peptide interactions in nanoporous substrate-supported lipid model membranes. Langmuir: the Acs Journal of Surfaces and Colloids 23(13): 7229-7234, 2007

Orientation and lipid-peptide interactions of gramicidin A in lipid membranes: polarized attenuated total reflection infrared spectroscopy and spin-label electron spin resonance. Biophysical Journal 86(3): 1521-1531, 2004

Phospholipid structure determines the effects of peptides on membranes. Differential scanning calorimetry studies with pentagastrin-related peptides. Biochimica et Biophysica Acta 856(2): 290-300, 1986

The Contribution of Differential Scanning Calorimetry for the Study of Peptide/Lipid Interactions. Methods in Molecular Biology 1964: 3-15, 2019

Interactions of starch and sugar water measured by electron spin resonance and differential scanning calorimetry. Cereal Chemistry 67(3): 286-291, 1990

Quick-freeze differential scanning calorimetry and saturation transfer electron spin resonance: novel techniques for assessing phase transitions in biological membranes. Biochemical and Biophysical Research Communications 153(1): 104-108, 1988

Lipid interactions in membranes of extremely halophilic bacteria. I. Electron spin resonance and dilatometric studies of bilayer structure. Biochemistry 13(24): 4906-4913, 1974

A high sensitivity differential scanning calorimetry study of the interaction between poloxamers and dimyristoylphosphatidylcholine and dipalmitoylphosphatidylcholine liposomes. International Journal of Pharmaceutics 182(1): 101-110, 1999

Application of electron spin resonance for investigating peptide-lipid interactions. Biochemical Society Transactions 29(3): A55, 2001

Application of electron spin resonance for investigating peptide-lipid interactions, and correlation with thermodynamics. Biochemical Society Transactions 29(Pt 4): 582-589, 2001

Spin-label electron paramagnetic resonance and differential scanning calorimetry studies of the interaction between mitochondrial succinate-ubiquinone and ubiquinol-cytochrome c reductases. Biochemistry 25(23): 7675-7682, 1986