USA As Represented by Secretary of the Navy

Massachusetts Institute of Technology

George P Anderson

Ellen R Goldman

J Matthew Mauro

Jinny Lin Liu

Daniel Zabetakis

Moungi G Bawendi

Hedi M Mattoussi

Vikram C Sundar

Igor L Medintz

Kendrick Turner

P Audrey Brozozog Lee

Frances S Ligler

Chris Rowe Taitt

Nadezhda V Kulagina

Banahalli R Ratna

Jawad Naciri

Christopher M Spillmann

Marc P Raphael

Joel P Golden

Thomas Pons

Thomas J Esparza

A number of single domain antibodies (sdAb, also known as nanobodies or VHH) were developed that bind nucleocapsid protein of the SARS-CoV-2 virus. They are useful for detecting the virus and could also find application in therapeutics.

Single domain antibodies to SARS-CoV-2 nucleocapsid protein

Described herein are nucleic acids encoding single-domain antibodies that might serve as alternatives to conventional monoclonal antibodies for either the detection or treatment of Chikungunya Virus (CHIKV).

Nucleic acids encoding single domain antibodies to chikungunya virus

Described herein are single-domain antibodies that might serve as alternatives to conventional monoclonal antibodies for either the detection or treatment of Chikungunya Virus (CHIKV).

Single domain antibodies to Chikungunya virus

A single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of &#x3b1;-synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

Single-domain antibody fusion proteins with the acid tail of alpha-synuclein

A nucleic acid encodes a single-domain antibody (sdAb) is produced by causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of &#x3b1;-synuclein. In embodiments, the protein is free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

Nucleic acids for single-domain antibodies with thermal stability under cytoplasmic expression

Methods of producing a single-domain antibody (sdAb) include causing a bacteria to express the sdAb into cytoplasm of the bacteria, wherein the sdAb is expressed as a fusion protein with the acid tail of &#x3b1;-synuclein; and then purifying the sdAb, wherein the fusion protein is expressed free of a periplasmic location tag. Such antibodies have the unexpected ability to refold after thermal denaturation.

Single-domain antibodies with improved thermal stability under cytoplasmic expression

Described herein are new recognition elements (antibodies or functional fragments thereof) that effectively bind to trinitrotoluene (TNT). Also disclosed is a single chain fragment recognition element.

Antibody and recombinant derivative for the detection of trinitrotoluene

Described herein is the development of recombinant single domain antibodies, also known as nanobodies, that may provide better therapeutic results or be useful for diagnostic applications of B-cell lymphomas, or in other applications where an antibody to CD20 may be useful.

Single domain antibodies that bind to human CD20

Genetic fusions of proteins, for example single-domain antibodies (sdAbs), with a positively-charged domain enhanced immobilization of active protein in a desired orientation.

Charged peptide appendage to facilitate oriented protein covalent immobilization

A nanoparticle having a surfactant shell with a hydrophilic outer surface and a hydrophobic inner surface and an organic chromophore and a polymer having aromatic groups within the surfactant shell. A method of making nanoparticles by: emulsifying an aqueous composition of a surfactant and an organic solution of a monomer and an organic chromophore to form micelles of the monomer and the chromophore inside a surfactant shell; and polymerizing the monomer. A method of: reacting a &#x3c9;-bromoalkyl acid with acryloyl acid lithium salt, and reacting the product with sodium hydride to produce an acryloyloxyalkyl carboxylic acid sodium salt. The compound shown below. 

Fluorescent organic nanoparticles

A method of biochemical identification by: providing a plurality of capture species bound to one or more substrates and suspected of having one or more biological targets affinity bound to at least one capture species; detecting which capture species contain bound biological targets to generate a binding pattern; and identifying the biological target based on the binding pattern. The capture species are independently selected from the group consisting of antimicrobial peptides, cytotoxic peptides, antibiotics, and combinations thereof. A device having the capture species bound to the substrates. At least two of the capture species are capable of multi-specific binding to one or more biological targets and may have overlapping but not identical affinity properties.

Affinity-based detection of biological targets

The ionic conjugates include an inorganic particle electrostatically associated with a macromolecule which can interact specifically with predetermined chemical species or biological targets.

Growing community of inventors

Bowie, MD, United States of America

George P Anderson