Influence of Cys-130 S. aureus Alpha-toxin on Planar Lipid Bilayer and Erythrocyte Membranes

Krasilnikov, Oleg V.; Yuldasheva, Liliya N.

doi:10.1007/s002329900198

Cited by 25 publications

(2 citation statements)

References 22 publications

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“…7). Consistent with these data, pH also alters the charge selectivity of the αHL pore (Table II; Krasilnikov et al 1997). For example, αHL is weakly anion selective at pH 7.5 (P K + / P Cl − = 0.77), more anion selective at pH 5.0 (P K + / P Cl − = 0.34), and cation selective at pH 11.0 (P K + / P Cl − = 2.2).…”

Section: Discussionsupporting

confidence: 73%

Prolonged Residence Time of a Noncovalent Molecular Adapter, β-Cyclodextrin, within the Lumen of Mutant α-Hemolysin Pores

Cheley

Bayley

2001

The Journal of General Physiology

109

133

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Noncovalent molecular adapters, such as cyclodextrins, act as binding sites for channel blockers when lodged in the lumen of the α-hemolysin (αHL) pore, thereby offering a basis for the detection of a variety of organic molecules with αHL as a sensor element. β-Cyclodextrin (βCD) resides in the wild-type αHL pore for several hundred microseconds. The residence time can be extended to several milliseconds by the manipulation of pH and transmembrane potential. Here, we describe mutant homoheptameric αHL pores that are capable of accommodating βCD for tens of seconds. The mutants were obtained by site-directed mutagenesis at position 113, which is a residue that lies near a constriction in the lumen of the transmembrane β barrel, and fall into two classes. Members of the tight-binding class, M113D, M113N, M113V, M113H, M113F and M113Y, bind βCD ∼104-fold more avidly than the remaining αHL pores, including WT-αHL. The lower K d values of these mutants are dominated by reduced values of koff. The major effect of the mutations is most likely a remodeling of the binding site for βCD in the vicinity of position 113. In addition, there is a smaller voltage-sensitive component of the binding, which is also affected by the residue at 113 and may result from transport of the neutral βCD molecule by electroosmotic flow. The mutant pores for which the dwell time of βCD is prolonged can serve as improved components for stochastic sensors.

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Section: Discussionsupporting

confidence: 73%

Prolonged Residence Time of a Noncovalent Molecular Adapter, β-Cyclodextrin, within the Lumen of Mutant α-Hemolysin Pores

Cheley

Bayley

2001

The Journal of General Physiology

109

133

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“…In particular the G130C-mutant has been shown to be fully active, with the cysteine translocating across the membrane during pore formation. 17,18,19,20,21 However, to our knowledge, there are only a few literature reports about making larger modifications to loop 128-131 . 22,23,24,25 It was shown for instance that substituting amino acids 130-134 with 5 histidines does not disrupt the pore forming ability of αHL and endows the pores with the ability to bind zinc ions, which blocks transport.…”

Section: Mainmentioning

confidence: 99%

Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins

Harjung,

Fracassi,

Devaraj

2023

Preprint

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A common method of generating artificial cells is to encapsulate protein expression systems within lipid vesicles. However, to communicate with the external environment, protein translocation across lipid membranes must take place. In living cells, protein transport across membranes is achieved with the aid of complex translocase systems which are difficult to reconstitute into artificial cells. Thus, there is need for simple mechanisms by which proteins can be encoded and expressed inside synthetic compartments yet still be externally displayed. Here we present a genetically encodable membrane functionalization system based on mutants of pore-forming proteins. We show that the membrane translocating loop of α-hemolysin can be engineered to translocate functional peptides up to 52 amino acids across lipid membranes. Engineered hemolysins can be used for genetically programming artificial cells to display interacting peptide pairs, enabling their assembly into artificial tissue-like structures capable of signal transduction.

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Bioinspired Ionic Diodes: From Unipolar to Bipolar

Huang

Kong

Wen

et al. 2018

Adv Funct Materials

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Bioinspired ionic diodes, as the building blocks for bioinspired ion channels, are extensively explored to mimic the ion transport functions of biological ion channels. Bioinspired nanochannels and nanopores are much more stable and robust than their biological counterparts and can be practically applied in many fields. This review summarizes the recent development of ionic diodes in both experimental and theoretical studies. First, the two types of ionic diodes, unipolar and bipolar, are introduced to give an overview of the nanofluidic field. Then, each type of ionic diode is described in detail and focuses on bipolar ionic diodes for their excellent control of ion transport. Furthermore, the applications of ionic diodes in sensing and energy conversion fields are summarized. In the last section, a perspective on the future development of ionic diodes is provided.

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Influence of Cys-130 S. aureus Alpha-toxin on Planar Lipid Bilayer and Erythrocyte Membranes

Cited by 25 publications

References 22 publications

Prolonged Residence Time of a Noncovalent Molecular Adapter, β-Cyclodextrin, within the Lumen of Mutant α-Hemolysin Pores

Prolonged Residence Time of a Noncovalent Molecular Adapter, β-Cyclodextrin, within the Lumen of Mutant α-Hemolysin Pores

Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins

Bioinspired Ionic Diodes: From Unipolar to Bipolar

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