4.6 Article

Thiol-based self-assembly nanostructures in promoting interfacial adhesion for copper-epoxy joint

Journal

APPLIED PHYSICS LETTERS
Volume 94, Issue 26, Pages -

Publisher

AMER INST PHYSICS
DOI: 10.1063/1.3167358

Keywords

adhesion; adhesive bonding; copper; fracture toughness; monolayers; nanostructured materials; polymers; self-assembly

Funding

  1. General Research Fund GRF [621907]

Ask authors/readers for more resources

Adhesion promotion between copper-epoxy interfaces without roughening the copper substrates is critical for new generation electronic devices. This paper demonstrates a pronounced adhesion promotion of a copper-epoxy joint from 4.8 J m(-2) for the untreated samples to 159 J m(-2) for the interfaces prepared with a thiol-based self-assembly molecular layer (SAM). The 33-fold improvement was related to the presence of nanostructures with the SAM treatment. The adhesion enhancement is attributed to both chemical bonding between copper and epoxy and the formation of nanosized features on copper substrates. The thiol promoter enhances the interfacial adhesion with no roughening of the substrates.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.6
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

Article Engineering, Biomedical

Trypsin-Instructed Self-Assembly on Endoplasmic Reticulum for Selectively Inhibiting Cancer Cells Dedicated to Professor George M. Whitesides on the occasion of his 80th birthday

Beom Jin Kim, Yu Fang, Hongjian He, Bing Xu

Summary: This study discovered a readily available peptide that selectively inhibits cancer cells by forming peptide assemblies on the endoplasmic reticulum (ER) through enzyme-instructed self-assembly (EISA), resulting in ER stress and eventual cell death. It offers a promising new strategy for potential cancer therapy by targeting cancer cell subcellular organelles.

ADVANCED HEALTHCARE MATERIALS (2021)

Article Biochemistry & Molecular Biology

Enzymatically forming cell compatible supramolecular assemblies of tryptophan-rich short peptides

Dongsik Yang, Beom Jin Kim, Hongjian He, Bing Xu

Summary: A new type of tryptophan-rich short peptides has been discovered, which act as hydrogelators, form supramolecular assemblies via enzymatic dephosphorylation, and exhibit cell compatibility. These peptides largely accumulate in lysosomes, are compatible with mammalian cells, and can transiently reduce the cytotoxicity of phenylalanine-rich peptide assemblies.

PEPTIDE SCIENCE (2021)

Article Biochemistry & Molecular Biology

Heterotypic Supramolecular Hydrogels Formed by Noncovalent Interactions in Inflammasomes

Adrianna N. Shy, Huaimin Wang, Zhaoqianqi Feng, Bing Xu

Summary: This study successfully developed new materials with the ability to form heterotypic peptide hydrogels using information revealed by structural biology. The ratio of complementary peptides affects the properties of the resulting hydrogels, while electrostatic interactions modulate the self-assembly process.

MOLECULES (2021)

Article Biochemical Research Methods

Peptide Assemblies Mimicking Chaperones for Protein Trafficking

Dongsik Yang, Hongjian He, Beom Jin Kim, Bing Xu

Summary: This study found that peptides with negatively charged peptides (NCPs) can self-assemble to form micelles at neutral or basic pH, facilitating the trafficking of histone proteins. Structure-activity studies revealed that self-assembly, proper stereochemistry, and acidic repeats are crucial for successful trafficking of H2B.

BIOCONJUGATE CHEMISTRY (2021)

Article Chemistry, Multidisciplinary

Enzymatic Assemblies of Thiophosphopeptides Instantly Target Golgi Apparatus and Selectively Kill Cancer Cells**

Weiyi Tan, Qiuxin Zhang, Jiaqing Wang, Meihui Yi, Hongjian He, Bing Xu

Summary: Introducing a sulfur atom into phosphopeptides enables rapid targeting of Golgi apparatus and selective killing of cancer cells. The resulting thiophosphopeptide self-assembles after alkaline phosphatase-catalyzed dephosphorylation, enters cells, and accumulates in Golgi apparatus, inhibiting cancer cells effectively.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2021)

Article Chemistry, Multidisciplinary

Dynamic Continuum of Nanoscale Peptide Assemblies Facilitates Endocytosis and Endosomal Escape

Hongjian He, Jiaqi Guo, Jiashu Xu, Jiaqing Wang, Shuang Liu, Bing Xu

Summary: This study demonstrates how nanoscale phosphopeptide assemblies cluster ALP to enable cellular uptake through caveolae-mediated endocytosis and endosomal escape. Dephosphorylation of phosphopeptides leads to the formation of peptidic nanofibers for endosomal escape. Inhibiting TNAP or disrupting lipid rafts abolishes the endocytosis process, while decreasing the transformation to nanofibers prevents endosomal escape.

NANO LETTERS (2021)

Article Chemistry, Organic

Synthesis and bioactivity of pyrrole-conjugated phosphopeptides

Qiuxin Zhang, Weiyi Tan, Bing Xu

Summary: In this study, we synthesized pyrrole-conjugated phosphopeptides and investigated their effects on cell viability. The results showed that the introduction of a heteroaromatic motif at the N-terminal of short peptides reduced their inhibitory activity against cancer cells and hindered morphological changes during enzymatic dephosphorylation.

BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY (2022)

Article Biochemical Research Methods

A Self-Assembling Probe for Imaging the States of Golgi Apparatus in Live Single Cells

Weiyi Tan, Qiuxin Zhang, Pengyu Hong, Bing Xu

Summary: This study utilizes an enzyme-instructed self-assembling thiophosphopeptide as a probe to reveal the state of the Golgi Apparatus (GA) in live cells. Results show that the probe accumulates in the GA at different rates depending on cell types and is sensitive to alkaline phosphatase expression. This self-assembling probe offers a novel approach for high-resolution imaging of subcellular organelles.

BIOCONJUGATE CHEMISTRY (2022)

Article Chemistry, Multidisciplinary

Enzyme-Responsive Peptide Thioesters for Targeting Golgi Apparatus

Weiyi Tan, Qiuxin Zhang, Monica C. Quinones-Frias, Alan Y. Hsu, Yichi Zhang, Avital Rodal, Pengyu Hong, Hongbo R. Luo, Bing Xu

Summary: This study demonstrates the effectiveness of unconventional peptide thioesters in selectively targeting the Golgi apparatus, thereby controlling cell fate. These peptide thioesters enter cells through specific endocytic pathways and accumulate in the Golgi apparatus, disrupting protein trafficking and leading to cell death.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2022)

Review Chemistry, Multidisciplinary

Enzymatic Noncovalent Synthesis for Targeting Subcellular Organelles

Qiuxin Zhang, Weiyi Tan, Bing Xu

Summary: Enzymatic noncovalent synthesis (ENS) is a mechanism that utilizes enzymatic reactions to produce spatially organized higher-order supramolecular assemblies, which can modulate cellular processes. This Review highlights the recent progress in the application of ENS for targeted subcellular organelles, showcasing its potential in understanding diseases, controlling cell behaviors, and developing new therapeutics.

CHEMPLUSCHEM (2022)

Article Chemistry, Multidisciplinary

Enzyme Responsive Rigid-Rod Aromatics Target Undruggable Phosphatases to Kill Cancer Cells in a Mimetic Bone Microenvironment

Meihui Yi, Fengbin Wang, Weiyi Tan, Jer-Tsong Hsieh, Edward H. Egelman, Bing Xu

Summary: This study demonstrates the use of enzymatic responsive rigid-rod aromatics as substrates to target undruggable phosphatases and kill cancer cells in a bone microenvironment. The compounds effectively kill metastatic prostate cancer cells and mimic osteoblast cells, with high cellular uptake rate.

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY (2022)

Article Chemistry, Multidisciplinary

Intranuclear Nanoribbons for Selective Killing of Osteosarcoma Cells

Shuang Liu, Qiuxin Zhang, Hongjian He, Meihui Yi, Weiyi Tan, Jiaqi Guo, Bing Xu

Summary: In this study, intranuclear nanoribbons formed by dephosphorylation of phosphorylated peptides catalyzed by alkaline phosphatase were demonstrated to selectively kill osteosarcoma cells. These peptides rapidly kill the cancer cells by interacting with histone proteins, while being nontoxic to normal cells.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2022)

Article Chemistry, Multidisciplinary

An Exploration of Multiple Component Peptide Assemblies by Enzyme-Instructed Self-Assembly

Adrianna N. Shy, Jiashu Xu, Beom Jin Kim, Bing Xu

Summary: This study focuses on the enzyme-instructed self-assembly (EISA) of a phosphopeptide (1P) derived from the protein crystal structures of Merlin and CRL4(DCAF-1). The results demonstrate that even with the presence of a hydrophilic peptide, 1P can form a hydrogel at a very low volume fraction. Additionally, diastereomer 2P and enantiomer 3P of 1P are able to form hydrogels via EISA at higher concentrations than 1P.

CHEMSYSTEMSCHEM (2023)

Article Chemistry, Multidisciplinary

Intramitochondrial co-assembly between ATP and nucleopeptides induces cancer cell apoptosis

Huyeon Choi, Gaeun Park, Eunhye Shin, Seon Woo Shin, Batakrishna Jana, Seongeon Jin, Sangpil Kim, Huaimin Wang, Sang Kyu Kwak, Bing Xu, Ja-Hyoung Ryu

Summary: Mitochondria-targeting nucleopeptide can sequester ATP by self-assembling, leading to apoptosis of cancer cells.

CHEMICAL SCIENCE (2022)

Review Chemistry, Multidisciplinary

Enzymatic noncovalent synthesis of peptide assemblies generates multimolecular crowding in cells for biomedical applications

Meihui Yi, Weiyi Tan, Jiaqi Guo, Bing Xu

Summary: Enzymatic noncovalent synthesis allows for the control of multimolecular crowding in cells, offering opportunities for modulating cellular functions and various biomedical applications.

CHEMICAL COMMUNICATIONS (2021)

No Data Available