Pretražite po imenu i prezimenu autora, mentora, urednika, prevoditelja

Napredna pretraga

Pregled bibliografske jedinice broj: 940331

Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides


Vazdar, Mario; Heyda, Jan; Mason, Philip E.; Tesei, Giulio; Allolio, Christoph; Lund, Mikael; Jungwirth, Pavel
Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides // Accounts of chemical research, 51 (2018), 6; 1455-1464 doi:10.1021/acs.accounts.8b00098 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 940331 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides

Autori
Vazdar, Mario ; Heyda, Jan ; Mason, Philip E. ; Tesei, Giulio ; Allolio, Christoph ; Lund, Mikael ; Jungwirth, Pavel

Izvornik
Accounts of chemical research (0001-4842) 51 (2018), 6; 1455-1464

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
guanidinium, ammonium, arginine, lysine, molecular simulations, cell penetrating peptides

Sažetak
It is a textbook knowledge that charges of the same polarity repel each other. For two monovalent ions in the gas phase at a close contact this repulsive interaction amounts to hundreds of kilojoules per mole. In aqueous solutions, however, this Coulomb repulsion is strongly attenuated by a factor equal to the dielectric constant of the medium. The residual repulsion, which now amounts only to units of kilojoules per mole, may be in principle offset by attractive interactions. Probably the smallest cationic pair, where a combination of dispersion and cavitation forces overwhelms the Coulomb repulsion, consists of two guanidinium ions in water. Indeed, by a combination of molecular dynamics with electronic structure calculations and electrophoretic, as well as spectroscopic, experiments, we have demonstrated that aqueous guanidinium cations form (weakly) thermodynamically stable like- charge ion pairs. The importance of pairing of guanidinium cations in aqueous solutions goes beyond a mere physical curiosity, since it has significant biochemical implications. Guanidinium chloride is known to be an efficient and flexible protein denaturant. This is due to the ability of the orientationally amphiphilic guanidinium cations to disrupt various secondary structural motifs of proteins by pairing promiscuously with both hydrophobic and hydrophilic groups, including guanidinium- containing side chains of arginines. The fact that the cationic guanidinium moiety forms the dominant part of the arginine side chain implies that the like-charge ion pairing may also play a role for interactions between peptides and proteins. Indeed, arginine– arginine pairing has been frequently found in structural protein databases. In particular, when strengthened by a presence of negatively charged glutamate, aspartate, or C-terminal carboxylic groups, this binding motif helps to stabilize peptide or protein dimers and is also found in or near active sites of several enzymes. The like-charge pairing of the guanidinium side-chain groups may also hold the key to the understanding of the arginine “magic”, that is, the extraordinary ability of arginine-rich polypeptides to passively penetrate across cellular membranes. Unlike polylysines, which are also highly cationic but lack the ease in crossing membranes, polyarginines do not exhibit mutual repulsion. Instead, they accumulate at the membrane, weaken it, and might eventually cross in a concerted, “train-like” manner. This behavior of arginine-rich cell penetrating peptides can be exploited when devising smart strategies how to deliver in a targeted way molecular cargos into the cell.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Projekt / tema
HRZZ-UIP-2014-09-6090 - Molekularni aspekti oksidativnih procesa u stanicama (MolOxStress) (Vazdar, Mario, HRZZ - 2014-09 )

Ustanove
Institut "Ruđer Bošković", Zagreb

Profili:

Avatar Url Mario Vazdar (autor)

Citiraj ovu publikaciju

Vazdar, Mario; Heyda, Jan; Mason, Philip E.; Tesei, Giulio; Allolio, Christoph; Lund, Mikael; Jungwirth, Pavel
Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides // Accounts of chemical research, 51 (2018), 6; 1455-1464 doi:10.1021/acs.accounts.8b00098 (međunarodna recenzija, članak, znanstveni)
Vazdar, M., Heyda, J., Mason, P., Tesei, G., Allolio, C., Lund, M. & Jungwirth, P. (2018) Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides. Accounts of chemical research, 51 (6), 1455-1464 doi:10.1021/acs.accounts.8b00098.
@article{article, year = {2018}, pages = {1455-1464}, DOI = {10.1021/acs.accounts.8b00098}, keywords = {guanidinium, ammonium, arginine, lysine, molecular simulations, cell penetrating peptides}, journal = {Accounts of chemical research}, doi = {10.1021/acs.accounts.8b00098}, volume = {51}, number = {6}, issn = {0001-4842}, title = {Arginine “Magic”: Guanidinium Like-Charge Ion Pairing from Aqueous Salts to Cell Penetrating Peptides}, keyword = {guanidinium, ammonium, arginine, lysine, molecular simulations, cell penetrating peptides} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


Citati





    Contrast
    Increase Font
    Decrease Font
    Dyslexic Font