Self-assembly behaviors of molecular designer functional RADA16-I peptides: influence of motifs, pH, and assembly time

Sun, Yuqiao; Zhang, Yongnu; Tian, Lingling; Zhao, Yuyuan; Wu, Dong; Wang, Xue; Ramakrishna, Seeram; Wu, Wutian; He, Liumin

doi:10.1088/1748-605x/12/1/015007

Cited by 27 publications

(34 citation statements)

References 39 publications

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“…One side of the RADA4 monomer is thought to consist predominantly of nonpolar hydrophobic Ala (A), and the other side of alternating oppositely charged amino acids, namely Arg (R) and Asp (D). Recent publications suggest that the surface net charge is a crucial physicochemical parameter in protein aggregation [183,184]. The latter work, based on CD analysis and metadynamics simulations, concludes that RADA16 fibrillation could be easily modulated by pH and ionic strength.…”

Section: Abbreviationsmentioning

confidence: 95%

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins

Bianchi

Longhi

Grandori

et al. 2020

IJMS

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The abundance of intrinsic disorder in the protein realm and its role in a variety of physiological and pathological cellular events have strengthened the interest of the scientific community in understanding the structural and dynamical properties of intrinsically disordered proteins (IDPs) and regions (IDRs). Attempts at rationalizing the general principles underlying both conformational properties and transitions of IDPs/IDRs must consider the abundance of charged residues (Asp, Glu, Lys, and Arg) that typifies these proteins, rendering them assimilable to polyampholytes or polyelectrolytes. Their conformation strongly depends on both the charge density and distribution along the sequence (i.e., charge decoration) as highlighted by recent experimental and theoretical studies that have introduced novel descriptors. Published experimental data are revisited herein in the frame of this formalism, in a new and possibly unitary perspective. The physicochemical properties most directly affected by charge density and distribution are compaction and solubility, which can be described in a relatively simplified way by tools of polymer physics. Dissecting factors controlling such properties could contribute to better understanding complex biological phenomena, such as fibrillation and phase separation. Furthermore, this knowledge is expected to have enormous practical implications for the design, synthesis, and exploitation of bio-derived materials and the control of natural biological processes.

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Section: Abbreviationsmentioning

confidence: 95%

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins

Bianchi

Longhi

Grandori

et al. 2020

IJMS

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“…As a classical ion-complementary self-assembling peptide, RADA16-I can assemble to form a b-folded secondary structure and form nanofibers, thus it has been widely used in various research fields. There are a hydrophilic surface with positively charged arginine (Arg, R) and negatively charged aspartic acid (Asp, D) and a hydrophobic surface with nonpolar amino acid alanine (Ala, A) in the structure of RADA16-I [45,46]. RADA16-I has shown some potentials to be carriers of hydrophobic compounds or drugs for its hydrophobic side can interact with a hydrophobic compounds or drugs, while its hydrophilic side can make the hydrophobic compound or drug relatively stable in aqueous solution systems [47,48].…”

Section: Peptide Designmentioning

confidence: 99%

The interaction between self – assembling peptides and emodin and the controlled release of emodin from in-situ hydrogel

Wei

Cui

Wang

et al. 2019

Artificial Cells, Nanomedicine, and Biotechnology

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Ion-complementary self-assembling peptides have potential in delivering hydrophobic drugs. This study involved two self-assembling peptides, RADA16-I and RVDV16-I, of which RVDV16-I was a novel selfassembling peptide with different hydrophobic side chains designed from RADA16-I. The purpose of this study was to observe the interaction between different self-assembling peptides and emodin through fluorescence spectrophotometry, CD, SEM and AFM; to construct a preliminary suspension in-situ hydrogel delivery system for emodin with the self-assembling peptides; and to investigate the drug-loading and drug-releasing properties of the self-assembling peptides on emodin. The results showed that both peptides can interact with emodin and the interaction was dominated by hydrophobic interaction. The aqueous solutions of both self-assembling peptides can form relatively stable suspensions with emodin under mechanical stirring, and the suspension can form in-situ hydrogel under physiological condition. In vitro release of emodin from the hydrogels showed a manner of sustained release to some extent. Cell viability studies showed inherent proliferation inhibiting effects of emodin on tumor cells was maintained or enhanced through the in-situ hydrogels. The self-assembling peptides RADA16-I and RVDV16-I had showed promising drug-loading and drug-releasing performance for hydrophobic drugs. It is reasonable to exploit self-assembling peptides as drug carriers for their great potential to improve delivery of hydrophobic drugs.

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“…β‐sheet content of RADA16‐I solution spectra at pH = 7 is significantly lower than the one at pH = 4 . Dimension of the RADA16‐I peptide fiber is also dependent on time and environmental factors …”

Section: Introductionmentioning

confidence: 96%

“…36,37 Dimension of the RADA16-I peptide fiber is also dependent on time and environmental factors. [38][39][40] Using experimental design methods such as RSM, it is possible to predict the effects of the operational factors and their interactions to obtain the optimized condition by performing minimal tests. 41,42 In this study, with passive particle tracking, we aim to investigate the motion of a particle in a mixture containing RADA16-I peptide, salt, and blood serum.…”

Section: Introductionmentioning

confidence: 99%

On the analysis of microrheological responses of self‐assembling RADA16‐I peptide hydrogel

Seyedkarimi

Mirzadeh

Bagheri‐Khoulenjani

2018

J Biomedical Materials Res

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This work aims to obtain a hydrogel based on self‐assembling RADA16‐I with proper rheological properties for hemostasis application. Response surface methodology (RSM) was performed to predict the gelation and stiffness of the hydrogel in different concentrations of peptide and NaCl in water and blood serum milieus. Particle tracking microrheology technique was used to evaluate Brownian motion of polystyrene particles in the peptide solutions to obtain their trajectories and measure the viscoelastic properties (G′′, G″, and tan δ). Formation of gel was influenced by the concentrations of peptide and salt and their interactions. Optimum response for maximizing elastic modulus was obtained in the presence of blood serum in comparison with water. Negative effect of excess amount of NaCl was predicted by RSM model and confirmed by animal study. Circular dichroism (CD) analysis showed formation of β‐sheet secondary structure in water. On the other hand, in the presence of blood serum, tertiary structure was formed. Dimensional characterization of peptide fibers was performed by means of AFM. Peptide self‐assembly in blood serum (pH around 7) which contains different ions, led to enhancing bonds between fibers, caused increasing the fiber diameter and length by 20 and 10 times, respectively. © 2018 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 330–338, 2019.

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Self-assembly behaviors of molecular designer functional RADA16-I peptides: influence of motifs, pH, and assembly time

Cited by 27 publications

References 39 publications

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins

Relevance of Electrostatic Charges in Compactness, Aggregation, and Phase Separation of Intrinsically Disordered Proteins

The interaction between self – assembling peptides and emodin and the controlled release of emodin from in-situ hydrogel

On the analysis of microrheological responses of self‐assembling RADA16‐I peptide hydrogel

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