9.3 Flashcards

(10 cards)

1
Q
  1. What is the basic structure of a typical antibody molecule?
A

It is a Y-shaped protein composed of two identical heavy chains and two identical light chains, with variable regions in the Fab (antigen-binding) segments and a constant Fc region for effector interactions.

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2
Q
  1. Which parts of the antibody mediate antigen binding and effector functions?
A

The Fab region binds to specific antigens, while the Fc region interacts with immune effector cells and complement proteins.

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3
Q
  1. What are the main formats of therapeutic antibodies?
A

Formats include full-length monospecific antibodies, bispecific antibodies, antibody fragments (e.g., Fab, scFv, nanobodies), and conjugated forms such as antibody-drug conjugates (ADCs) and immunotoxins.

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4
Q
  1. How do bispecific antibodies differ from conventional monospecific antibodies?
A

Bispecific antibodies are engineered to bind two different epitopes or antigens simultaneously, whereas monospecific antibodies bind only a single target.

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5
Q
  1. What are common mechanisms of action for therapeutic antibodies?
A

They work by neutralizing target antigens, blocking receptor-ligand interactions, inducing cell death via antibody-dependent cellular cytotoxicity (ADCC) or complement-dependent cytotoxicity (CDC), and delivering conjugated toxins or radioisotopes.

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6
Q
  1. How does antibody-dependent cellular cytotoxicity (ADCC) function?
A

In ADCC, the antibody’s Fc region binds to Fc receptors on effector cells (like NK cells), triggering the lysis of the target cell bound by the antibody’s Fab region.

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7
Q
  1. What are some challenges associated with developing therapeutic antibodies?
A

Challenges include high production costs, complex manufacturing, potential immunogenicity, stability and storage issues, and limitations in administration routes (often injectable).

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8
Q
  1. How can immunogenicity of therapeutic antibodies be reduced?
A

By using humanized or fully human antibodies, engineering the Fc region, and modifying glycosylation to reduce immune recognition.

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9
Q
  1. What strategies are used to build better or different therapeutic antibodies?
A

Approaches include Fc engineering for enhanced effector function or half-life, developing bispecific/multi-specific formats, creating antibody-drug conjugates for targeted cytotoxicity, and using antibody fragments for improved tissue penetration.

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10
Q
  1. Why are antibody-drug conjugates (ADCs) significant in therapy?
A

ADCs couple the targeting specificity of antibodies with potent cytotoxic agents, ensuring selective drug delivery to diseased cells while minimizing damage to healthy tissues.

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