Structure-based design of functional amyloid materials.

نویسندگان

  • Dan Li
  • Eric M Jones
  • Michael R Sawaya
  • Hiroyasu Furukawa
  • Fang Luo
  • Magdalena Ivanova
  • Stuart A Sievers
  • Wenyuan Wang
  • Omar M Yaghi
  • Cong Liu
  • David S Eisenberg
چکیده

Amyloid fibers, once exclusively associated with disease, are acquiring utility as a class of biological nanomaterials. Here we introduce a method that utilizes the atomic structures of amyloid peptides, to design materials with versatile applications. As a model application, we designed amyloid fibers capable of capturing carbon dioxide from flue gas, to address the global problem of excess anthropogenic carbon dioxide. By measuring dynamic separation of carbon dioxide from nitrogen, we show that fibers with designed amino acid sequences double the carbon dioxide binding capacity of the previously reported fiber formed by VQIVYK from Tau protein. In a second application, we designed fibers that facilitate retroviral gene transfer. By measuring lentiviral transduction, we show that designed fibers exceed the efficiency of polybrene, a commonly used enhancer of transduction. The same procedures can be adapted to the design of countless other amyloid materials with a variety of properties and uses.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Nanomechanics of functional and pathological amyloid materials.

Amyloid or amyloid-like fibrils represent a general class of nanomaterials that can be formed from many different peptides and proteins. Although these structures have an important role in neurodegenerative disorders, amyloid materials have also been exploited for functional purposes by organisms ranging from bacteria to mammals. Here we review the functional and pathological roles of amyloid m...

متن کامل

Enzymatically Active Microgels from Self-Assembling Protein Nanofibrils for Microflow Chemistry

Amyloid fibrils represent a generic class of protein structure associated with both pathological states and with naturally occurring functional materials. This class of protein nanostructure has recently also emerged as an excellent foundation for sophisticated functional biocompatible materials including scaffolds and carriers for biologically active molecules. Protein-based materials offer th...

متن کامل

Strong underwater adhesives made by self-assembling multi-protein nanofibres.

Many natural underwater adhesives harness hierarchically assembled amyloid nanostructures to achieve strong and robust interfacial adhesion under dynamic and turbulent environments. Despite recent advances, our understanding of the molecular design, self-assembly and structure-function relationships of these natural amyloid fibres remains limited. Thus, designing biomimetic amyloid-based adhesi...

متن کامل

Study of Cis–trans Isomerization Mechanism of [3-(3-Aminomethyl) Phenylazo] Phenyl Acetic Acid as a Causative Role in Alzheimer Using Density Functional Theory

Amyloid-β (Aβ) self-assembly into cross-β amyloidfibrils is implicated in a causative role in Alzheimer’s disease pathology.Uncertainties persist regarding the mechanisms of amyloid self assembly and the role of metastable prefibrillar aggregates. Aβ fibrilsfeature a sheet-turn-sheet motif in the constituent β-strands; as such, turn nucleation has been proposed as a rate-limiting step in the se...

متن کامل

Preparation and study of the inhibitory effect of nano-niosomes containing essential oil from artemisia absinthium on amyloid fibril formation

Objective(s): Artemisia absinthium is an aromatic, perennial small shrub that shows multiple medical benefits, including anticancerous, neuroprotective, antifungal, hepatoprotective, antidepressant and antioxidant properties. One of the effective approaches to treat Alzheimer’s disease is targeting amyloid aggregation by antiamyloid drugs. In the current research study, an excellent grouping of...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Journal of the American Chemical Society

دوره 136 52  شماره 

صفحات  -

تاریخ انتشار 2014