Biophys J. PMID: 32160747. PMID: 32336099. Fitting to two adjacent lipids (one 13C to two 31P) gave similar results (SI Appendix, Fig. 2020 Mar 10;118(5):1044-1057. doi: 10.1016/j.bpj.2020.01.016. Epub ahead of print. (F) The equivalent τs vs. pH plots for POPC-only controls. 0000003277 00000 n PMID: 32040508; PMCID: PMC7034923. The fatty acid composition, i.e., saturated chain in the sn-1 position and unsaturated chain in the sn-2 position, mimics mammalian phospholipid composition. Next, the pH-specific microsecond timescale correlation times are shown in Fig. Epub 2020 Mar 29. Epub ahead of print. PMID: 32032504; PMCID: PMC7063487. J Cell Biol. Nano Lett. Biochim Biophys Acta Biomembr. PMID: 32005774. PMID: 32564617. In the critical third stage from pH 6.1 to 5.8, pHLIP extends from the bent configuration to become a TM helix (different from the final state III). FPK4 was reconstituted into POPC/POPG (4:1), DOPC/DOPG (4:1), and DOPE membranes at a peptide/lipid molar ratio of 1:20. Langmuir. Parigoris E, Dunkelmann DL, Murphy A, Wili N, Kaech A, Dumrese C, Jimenez-Rojo N, Silvan U. Facile generation of giant unilamellar vesicles using polyacrylamide gels. The answer to this question is critically important for understanding pHLIP−cell interactions at tumor acidity, which has an extracellular pH around 6.5 to 7.0 (24) and cell surface pH around 6.1 to 6.5 (25). PLoS Biol. S7. PMID: 32316569; PMCID: PMC7226168. For the population count CPU instruction, see, "Nanodisc Technology: Soluble Lipid Bilayer Systems for Structural and Functional Studies of Membrane Proteins",, Pages using collapsible list with both background and text-align in titlestyle, Articles containing unverified chemical infoboxes, Creative Commons Attribution-ShareAlike License, This page was last edited on 24 June 2020, at 14:46. S6). 2020 May;544:31-41. doi: 10.1016/j.virol.2020.02.006. We examine the effect of lipids on structure and dynamics of the CD3 ζζ dimer. R.T. is a guest editor invited by the Editorial Board. Together with the A13 distance of 7.8 Å, these data place the A13−D14 segment at the interface between the head groups and the alkyl chains, going away from the phosphates of the outer leaflet lipids. Epub 2020 Apr 4. Langmuir. The overall results clearly indicate that the membrane locations of D/E residues at any of these intervening pH values are significantly different from either state II or state III. It is a diacylglycerol and phospholipid. Sci Rep. 2020 Jun 11;10(1):9477. doi: 10.1038/s41598-020-66373-3. 2020 Mar 11;12(3):E637. Molecules. 2020 Jun 22:e2000746. 0000002624 00000 n 0000004673 00000 n 2020 Apr 21;36(15):4071-4079. doi: 10.1021/acs.langmuir.0c00456. At pH 7.4, all D/E residues, from the N-terminal E3 to the C-terminal E34, were only 5 Å to 7 Å away from the nearest 31P. 0000004833 00000 n Epub ahead of print. Previously, we hypothesized that such thermodynamic intermediate states differ from each other, as well as the initial and end states, by the protonation status of several D/E residues (30). Curr Protoc Protein Sci. J Nucl Med. Shedding Light on Metal-Based Nanoparticles in Zebrafish by Computed Tomography with Micrometer Resolution. Bryce DA, Kitt JP, Myres GJ, Harris JM. Revealing the mode of action of halictine antimicrobial peptides: a comprehensive study with model membranes. Interestingly, the two-population fittings for residues E3 and D14 at pH 6.4 show distinct best-fit distances for the D33-protonated and D33-deprotonated populations (Table 2), which may correlate with the two different secondary structures previously observed in the N-terminal region at this pH (23). PMID: 32533918. Generally, these interactions are supposed to involve the hydrophobic side chains protruding from the transmembrane helices. The experimental pH values were chosen based on the pKa values of D residues, for the purpose of reducing protonation state heterogeneity. Maravilla E, Le DP, Tran JJ, Chiu MH, Prenner EJ, Weers PMM. 0000048913 00000 n Epub ahead of print. Pham QD, Carlström G, Lafon O, Sparr E, Topgaard D. Quantification of the amount of mobile components in intact stratum corneum with natural-abundance 13C solid-state NMR. Kim M, Heinrich F, Haugstad G, Yu G, Yuan G, Satija SK, Zhang W, Seo HS, Metzger JM, Azarin SM, Lodge TP, Hackel BJ, Bates FS. doi: 10.3390/v12060668. InChI=1S/C42H82NO8P/c1-6-8-10-12-14-16-18-20-21-23-25-27-29-31-33-35-42(45)51-40(39-50-52(46,47)49-37-36-43(3,4)5)38-48-41(44)34-32-30-28-26-24-22-19-17-15-13-11-9-7-2/h20-21,40H,6-19,22-39H2,1-5H3/b21-20-/t40-/m1/s1, CCCCCCCCCCCCCCCC(=O)OC[C@H](COP(=O)([O-])OCC[N+](C)(C)C)OC(=O)CCCCCCC/C=C\CCCCCCCC, Except where otherwise noted, data are given for materials in their, This article is about the chemical. Viruses. Analyzing the CD3 ζζ–lipid contacts in the POPC and POPC… PMID: 32202793. 2020 Mar 21;229:104909. doi: 10.1016/j.chemphyslip.2020.104909. Lipid vesicles were formed from zwitterionic 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and negatively charged 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoethanolamine (POPE) in phosphate buffer (PBS). Epub 2020 Jan 28. PMID: 32804507. Ultrasound-mediated delivery enhances therapeutic efficacy of MMP sensitive liposomes. Epub 2020 Apr 9. PMID: 32364747. [1] It is available commercially synthetically[2] and is naturally present in eukaryotic cell membranes. For each peptide, the REDOR measurements were carried out at (A) pH 7.4, (B) 6.4, (C) 6.1, (D) 5.8 and (E) 5.3. The two-population fitting of the 13C−31P distances for individual D/E residues at pH 6.4 and 5.8 are shown in SI Appendix, Fig. 2020 Jun 2. doi: 10.1039/d0cp00450b. For instance, residues D31, D33, and E34 were in close proximity (i.e., distance of 5 Å to 7 Å) to 31P at both pH 7.4 and pH 5.3 (Fig. The fluorescence emission spectra were analyzed for both: suspension of liposomes with nanoparticles and for supported lipid bilayers containing QD on PEM. 2020 Apr 15;31(4):1156-1166. doi: 10.1021/acs.bioconjchem.0c00080. Cartoon models in D and F Insets depict the primary motions that contribute to the relaxation. Roussel G, White SH. Liu KN, Boxer SG. Ocul Surf. 2020 Jun 1;219(6):e201905085. The long chain lipids differ only in their headgroup structure and charge Fig. Nature. PMID: 32097623. 2020 May 15. doi: 10.1021/acs.langmuir.0c01000. Thus, the results at the intervening pH values could not have come from mixtures of state II and state III. Martinez-Calle M, Prieto M, Olmeda B, Fedorov A, Loura LMS, Pérez-Gil J. Nigam P. Equilibrium penetration of pluronic F-68 in lipid monolayers. 2020 Apr 11. doi: 10.1096/fj.202000107R. The SecA ATPase motor protein binds to Escherichia coli liposomes only as monomers. Deposition of liposomes and liposomes with quantum dots on polyelectrolyte films was studied in situ using quartz crystal microbalance with dissipation (QCM-D) technique. 3A), while both residues remain deprotonated at pH 6.4. 0000016450 00000 n Nat Chem Biol. 1) 100% popg. 0000006212 00000 n My current approach is to place explicit POPC lipids around the TM protein. Dey S, Das A, Dey A, Maiti S. Membrane affinity of individual toxic protein oligomers determined at the single-molecule level. 2020 May 3;12(5):1049. doi: 10.3390/polym12051049. 2 and Table 1), albeit presumably to different lipid layers (i.e., outer leaflet at pH 7.4, inner leaflet at pH 5.3), yet these C-terminal D residues showed no REDOR dephasing (i.e., >9 Å away) at all at pH 6.1 (Fig. Fig. 0000003852 00000 n PMID: 32160532. 2020 Apr 7;36(13):3393-3403. doi: 10.1021/acs.langmuir.9b03208. Structural Basis for Lipid Binding and Function by an Evolutionarily Conserved Protein, Serum Amyloid A. J Mol Biol. Biophys J. Thus, the second point is that the protonations of D31 and D33 not only induce local changes in the C-terminal region but also seem to trigger changes in N-terminal region around residues A10−D14. Life (Basel). Hi, I want to dock a protein to a TM protein embedded in a lipid bilayer. 0000011140 00000 n 2020 Apr 7;36(13):3600-3610. doi: 10.1021/acs.langmuir.9b03957. The original pH low insertion peptide (pHLIP, NH2-GGEQNPIYWARYADWLFTTP-LLLLDLALLVDADEGT-CO2H) is derived from the transmembrane (TM) helix C of bacteriorhodopsin (1).